![\"Loading..\"](\"//bibbase.org/img/ajax-loader.gif\")
\n\n\n generated by\n \n ![\"bibbase.org\"\n](\"//bibbase.org/img/logo.svg\"\n "\\"BibBase")
\n \n
\n \n\n \n \n \n\n
\n\n\n - \n\n
- \n \n Group by\n \n \n
- \n
- \n Year\n \n
- \n Author\n \n
- \n Type\n \n
- \n Keyword\n \n
- \n Downloads\n \n
\n\n\n - \n \n \n \n \n
- \n
- \n \n Expand/Collapse All\n \n \n
- \n \n Download BibTeX\n \n \n
- \n \n RSS Feed\n \n \n
\n\n \n\n\n \n
\n\n Excellent! Next you can\n create a new website with this list, or\n embed it in an existing web page by copying & pasting\n any of the following snippets.\n\n
\n\n \n JavaScript\n (easiest)\n
\n \n
\n\n PHP\n \n <script src=\"https://bibbase.org/show?bib=https%3A%2F%2Fsossogroup.uk%2Fwp-content%2Fuploads%2F2020%2F06%2Ficebio_website_2.0.bib&jsonp=1&jsonp=1\"></script>\n \n \n
\n\n iFrame\n (not recommended)\n \n <?php\n $contents = file_get_contents(\"https://bibbase.org/show?bib=https%3A%2F%2Fsossogroup.uk%2Fwp-content%2Fuploads%2F2020%2F06%2Ficebio_website_2.0.bib&jsonp=1\");\n print_r($contents);\n ?>\n \n \n
\n\n \n <iframe src=\"https://bibbase.org/show?bib=https%3A%2F%2Fsossogroup.uk%2Fwp-content%2Fuploads%2F2020%2F06%2Ficebio_website_2.0.bib&jsonp=1\"></iframe>\n \n \n For more details see the documention.\n
\n\n\n This is a preview! To use this list on your own web site\n or create a new web site from it,\n create a free account. The file will be added\n and you will be able to edit it in the File Manager.\n We will show you instructions once you've created your account.\n
\n\n \n\n
\n\n To the site owner:
\n\nAction required! Mendeley is changing its\n API. In order to keep using Mendeley with BibBase past April\n 14th, you need to:\n
- \n
- renew the authorization for BibBase on Mendeley, and \n
- update the BibBase URL\n in your page the same way you did when you initially set up\n this page.\n \n
\n \n \n Fix it now\n
\n\n \n \n
\n\n\n \n\n \n \n \n \n\n\n
\n\n \n \n 2020\n \n \n (7)\n \n \n
\n \n \n \n
\n \n \n\n \n \n \n \n \n \n Insights into the Emerging Networks of Voids in Simulated Supercooled Water.\n \n \n \n \n\n\n \n Ansari, N.; Onat, B.; Sosso, G. C.; and Hassanali, A.\n\n\n \n\n\n\n J. Phys. Chem. B, 124(11): 2180–2190. March 2020.\n Publisher: American Chemical Society\n\n\n\n
\n\n\n\n \n \n![\"Insights](\"//bibbase.org/img/filetypes/link.svg\"\n\t "\\"Paper\\"\n\t")
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n@article{ansari_insights_2020,\n\ttitle = {Insights into the {Emerging} {Networks} of {Voids} in {Simulated} {Supercooled} {Water}},\n\tvolume = {124},\n\tissn = {1520-6106},\n\turl = {https://doi.org/10.1021/acs.jpcb.9b10144},\n\tdoi = {10.1021/acs.jpcb.9b10144},\n\tabstract = {The structural evolution of supercooled liquid water as we approach the glass transition temperature continues to be an active area of research. Here, we use molecular dynamics simulations of TIP4P/ice water to study the changes in the connected regions of empty space within the liquid, which we investigate using the Voronoi-voids network. We observe two important features: supercooling enhances the fraction of nonspherical voids and different sizes of voids tend to cluster forming a percolating network. By examining order parameters such as the local structure index (LSI), tetrahedrality and topological defects, we show that water molecules near large void clusters tend to be slightly more tetrahedral than those near small voids, with a lower population of under- and overcoordinated defects. We show further that the distribution of closed rings of water molecules around small and large void clusters maintain a balance between 6 and 7 membered rings. Our results highlight the changes of the dual voids and water network as a structural hallmark of supercooling and provide insights into the molecular origins of cooperative effects underlying density fluctuations on the subnanometer and nanometer length scale. In addition, the percolation of the voids and the hydrogen bond network around the voids may serve as useful order parameters to investigate density fluctuations in supercooled water.},\n\tnumber = {11},\n\turldate = {2020-06-03},\n\tjournal = {J. Phys. Chem. B},\n\tauthor = {Ansari, Narjes and Onat, Berk and Sosso, Gabriele C. and Hassanali, Ali},\n\tmonth = mar,\n\tyear = {2020},\n\tnote = {Publisher: American Chemical Society},\n\tpages = {2180--2190}\n}\n\n\n\n The structural evolution of supercooled liquid water as we approach the glass transition temperature continues to be an active area of research. Here, we use molecular dynamics simulations of TIP4P/ice water to study the changes in the connected regions of empty space within the liquid, which we investigate using the Voronoi-voids network. We observe two important features: supercooling enhances the fraction of nonspherical voids and different sizes of voids tend to cluster forming a percolating network. By examining order parameters such as the local structure index (LSI), tetrahedrality and topological defects, we show that water molecules near large void clusters tend to be slightly more tetrahedral than those near small voids, with a lower population of under- and overcoordinated defects. We show further that the distribution of closed rings of water molecules around small and large void clusters maintain a balance between 6 and 7 membered rings. Our results highlight the changes of the dual voids and water network as a structural hallmark of supercooling and provide insights into the molecular origins of cooperative effects underlying density fluctuations on the subnanometer and nanometer length scale. In addition, the percolation of the voids and the hydrogen bond network around the voids may serve as useful order parameters to investigate density fluctuations in supercooled water.\n
\n\n\n\n \n\n \n \n \n \n \n \n Polyampholytes as Emerging Macromolecular Cryoprotectants.\n \n \n \n \n\n\n \n Stubbs, C.; Bailey, T. L.; Murray, K.; and Gibson, M. I.\n\n\n \n\n\n\n Biomacromolecules, 21(1): 7–17. January 2020.\n Publisher: American Chemical Society\n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n@article{stubbs_polyampholytes_2020,\n\ttitle = {Polyampholytes as {Emerging} {Macromolecular} {Cryoprotectants}},\n\tvolume = {21},\n\tissn = {1525-7797},\n\turl = {https://doi.org/10.1021/acs.biomac.9b01053},\n\tdoi = {10.1021/acs.biomac.9b01053},\n\tabstract = {Cellular cryopreservation is a platform technology which underpins cell biology, biochemistry, biomaterials, diagnostics, and the cold chain for emerging cell-based therapies. This technique relies on effective methods for banking and shipping to avoid the need for continuous cell culture. The most common method to achieve cryopreservation is to use large volumes of organic solvent cryoprotective agents which can promote either a vitreous (ice free) phase or dehydrate and protect the cells. These methods are very successful but are not perfect: not all cell types can be cryopreserved and recovered, and the cells do not always retain their phenotype and function post-thaw. This Perspective will introduce polyampholytes as emerging macromolecular cryoprotective agents and demonstrate they have the potential to impact a range of fields from cell-based therapies to basic cell biology and may be able to improve, or replace, current solvent-based cryoprotective agents. Polyampholytes have been shown to be remarkable (mammalian cell) cryopreservation enhancers, but their mechanism of action is unclear, which may include membrane protection, solvent replacement, or a yet unknown protective mechanism, but it seems the modulation of ice growth (recrystallization) may only play a minor role in their function, unlike other macromolecular cryoprotectants. This Perspective will discuss their synthesis and summarize the state-of-the-art, including hypotheses of how they function, to introduce this exciting area of biomacromolecular science.},\n\tnumber = {1},\n\turldate = {2020-06-11},\n\tjournal = {Biomacromolecules},\n\tauthor = {Stubbs, Christopher and Bailey, Trisha L. and Murray, Kathryn and Gibson, Matthew I.},\n\tmonth = jan,\n\tyear = {2020},\n\tnote = {Publisher: American Chemical Society},\n\tpages = {7--17},\n\tfile = {ACS Full Text Snapshot:/Users/wolf/Zotero/storage/QT3Z5NHT/acs.biomac.html:text/html;Full Text PDF:/Users/wolf/Zotero/storage/KIACXPQ5/Stubbs et al. - 2020 - Polyampholytes as Emerging Macromolecular Cryoprot.pdf:application/pdf}\n}\n\n\n\n Cellular cryopreservation is a platform technology which underpins cell biology, biochemistry, biomaterials, diagnostics, and the cold chain for emerging cell-based therapies. This technique relies on effective methods for banking and shipping to avoid the need for continuous cell culture. The most common method to achieve cryopreservation is to use large volumes of organic solvent cryoprotective agents which can promote either a vitreous (ice free) phase or dehydrate and protect the cells. These methods are very successful but are not perfect: not all cell types can be cryopreserved and recovered, and the cells do not always retain their phenotype and function post-thaw. This Perspective will introduce polyampholytes as emerging macromolecular cryoprotective agents and demonstrate they have the potential to impact a range of fields from cell-based therapies to basic cell biology and may be able to improve, or replace, current solvent-based cryoprotective agents. Polyampholytes have been shown to be remarkable (mammalian cell) cryopreservation enhancers, but their mechanism of action is unclear, which may include membrane protection, solvent replacement, or a yet unknown protective mechanism, but it seems the modulation of ice growth (recrystallization) may only play a minor role in their function, unlike other macromolecular cryoprotectants. This Perspective will discuss their synthesis and summarize the state-of-the-art, including hypotheses of how they function, to introduce this exciting area of biomacromolecular science.\n
\n\n\n\n \n\n \n \n \n \n \n \n Combinatorial Biomaterials Discovery Strategy to Identify New Macromolecular Cryoprotectants.\n \n \n \n \n\n\n \n Stubbs, C.; Murray, K. A.; Ishibe, T.; Mathers, R. T.; and Gibson, M. I.\n\n\n \n\n\n\n ACS Macro Lett., 9(2): 290–294. February 2020.\n Publisher: American Chemical Society\n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n@article{stubbs_combinatorial_2020,\n\ttitle = {Combinatorial {Biomaterials} {Discovery} {Strategy} to {Identify} {New} {Macromolecular} {Cryoprotectants}},\n\tvolume = {9},\n\turl = {https://doi.org/10.1021/acsmacrolett.0c00044},\n\tdoi = {10.1021/acsmacrolett.0c00044},\n\tabstract = {Cryoprotective agents (CPAs) are typically solvents or small molecules, but there is a need for innovative CPAs to reduce~toxicity and increase cell yield, for the banking and transport of cells. Here we use a photochemical high-throughput discovery platform to identify macromolecular cryoprotectants, as rational design approaches are currently limited by the lack of structure{\\textendash}property relationships. Using liquid handling systems, 120 unique polyampholytes were synthesized using photopolymerization with RAFT agents. Cryopreservation screening identified {\\textquotedblleft}hit{\\textquotedblright} polymers and nonlinear trends between composition and function, highlighting the requirement for screening, with polymer aggregation being a key factor. The most active polymers reduced the volume of dimethyl sulfoxide (DMSO) required to cryopreserve a nucleated cell line, demonstrating the potential of this approach to identify materials for cell storage and transport.},\n\tnumber = {2},\n\turldate = {2020-06-11},\n\tjournal = {ACS Macro Lett.},\n\tauthor = {Stubbs, Christopher and Murray, Kathryn A. and Ishibe, Toru and Mathers, Robert T. and Gibson, Matthew I.},\n\tmonth = feb,\n\tyear = {2020},\n\tnote = {Publisher: American Chemical Society},\n\tpages = {290--294},\n\tfile = {ACS Full Text Snapshot:/Users/wolf/Zotero/storage/S96FUR53/acsmacrolett.html:text/html;Full Text PDF:/Users/wolf/Zotero/storage/7GG24AT2/Stubbs et al. - 2020 - Combinatorial Biomaterials Discovery Strategy to I.pdf:application/pdf}\n}\n\n\n\n Cryoprotective agents (CPAs) are typically solvents or small molecules, but there is a need for innovative CPAs to reduce~toxicity and increase cell yield, for the banking and transport of cells. Here we use a photochemical high-throughput discovery platform to identify macromolecular cryoprotectants, as rational design approaches are currently limited by the lack of structure–property relationships. Using liquid handling systems, 120 unique polyampholytes were synthesized using photopolymerization with RAFT agents. Cryopreservation screening identified “hit” polymers and nonlinear trends between composition and function, highlighting the requirement for screening, with polymer aggregation being a key factor. The most active polymers reduced the volume of dimethyl sulfoxide (DMSO) required to cryopreserve a nucleated cell line, demonstrating the potential of this approach to identify materials for cell storage and transport.\n
\n\n\n\n \n\n \n \n \n \n \n \n X-ray diffraction to probe the kinetics of ice recrystallization inhibition.\n \n \n \n \n\n\n \n Fayter, A.; Huband, S.; and Gibson, M. I.\n\n\n \n\n\n\n Analyst, 145(10): 3666–3677. May 2020.\n Publisher: The Royal Society of Chemistry\n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n@article{fayter_x-ray_2020,\n\ttitle = {X-ray diffraction to probe the kinetics of ice recrystallization inhibition},\n\tvolume = {145},\n\tissn = {1364-5528},\n\turl = {https://pubs.rsc.org/en/content/articlelanding/2020/an/c9an02141h},\n\tdoi = {10.1039/C9AN02141H},\n\tabstract = {Understanding the nucleation and growth of ice is crucial in fields ranging from infrastructure maintenance, to the environment, and to preserving biologics in the cold chain. Ice binding and antifreeze proteins are potent ice recrystallization inhibitors (IRI), and synthetic materials that mimic this function have emerged, which may find use in biotechnology. To evaluate IRI activity, optical microscopy tools are typically used to monitor ice grain size either by end-point measurements or as a function of time. However, these methods provide 2-dimensional information and image analysis is required to extract the data. Here we explore using wide angle X-ray scattering (WAXS/X-ray powder diffraction (XRD)) to interrogate 100's of ice crystals in 3-dimensions as a function of time. Due to the random organization of the ice crystals in the frozen sample, the number of orientations measured by XRD is proportional to the number of ice crystals, which can be measured as a function of time. This method was used to evaluate the activity for a panel of known IRI active compounds, and shows strong agreement with results obtained from cryo-microscopy, as well as being advantageous in that time-dependent ice growth is easily extracted. Diffraction analysis also confirmed, by comparing the obtained diffraction patterns of both ice binding and non-binding additives, that the observed hexagonal ice diffraction patterns obtained cannot be used to determine which crystal faces are being bound. This method may help in the discovery of new IRI active materials as well as enabling kinetic analysis of ice growth.},\n\tlanguage = {en},\n\tnumber = {10},\n\turldate = {2020-06-11},\n\tjournal = {Analyst},\n\tauthor = {Fayter, Alice and Huband, Steven and Gibson, Matthew I.},\n\tmonth = may,\n\tyear = {2020},\n\tnote = {Publisher: The Royal Society of Chemistry},\n\tpages = {3666--3677},\n\tfile = {Full Text PDF:/Users/wolf/Zotero/storage/4RWIGSHD/Fayter et al. - 2020 - X-ray diffraction to probe the kinetics of ice rec.pdf:application/pdf;Snapshot:/Users/wolf/Zotero/storage/E8TUDABH/c9an02141h.html:text/html}\n}\n\n\n\n Understanding the nucleation and growth of ice is crucial in fields ranging from infrastructure maintenance, to the environment, and to preserving biologics in the cold chain. Ice binding and antifreeze proteins are potent ice recrystallization inhibitors (IRI), and synthetic materials that mimic this function have emerged, which may find use in biotechnology. To evaluate IRI activity, optical microscopy tools are typically used to monitor ice grain size either by end-point measurements or as a function of time. However, these methods provide 2-dimensional information and image analysis is required to extract the data. Here we explore using wide angle X-ray scattering (WAXS/X-ray powder diffraction (XRD)) to interrogate 100's of ice crystals in 3-dimensions as a function of time. Due to the random organization of the ice crystals in the frozen sample, the number of orientations measured by XRD is proportional to the number of ice crystals, which can be measured as a function of time. This method was used to evaluate the activity for a panel of known IRI active compounds, and shows strong agreement with results obtained from cryo-microscopy, as well as being advantageous in that time-dependent ice growth is easily extracted. Diffraction analysis also confirmed, by comparing the obtained diffraction patterns of both ice binding and non-binding additives, that the observed hexagonal ice diffraction patterns obtained cannot be used to determine which crystal faces are being bound. This method may help in the discovery of new IRI active materials as well as enabling kinetic analysis of ice growth.\n
\n\n\n\n \n\n \n \n \n \n \n \n Ice recrystallisation inhibiting polymer nano-objects via saline-tolerant polymerisation-induced self-assembly.\n \n \n \n \n\n\n \n Georgiou, P. G.; Kontopoulou, I.; Congdon, T. R.; and Gibson, M. I.\n\n\n \n\n\n\n Mater. Horiz.. May 2020.\n Publisher: The Royal Society of Chemistry\n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n@article{georgiou_ice_2020,\n\ttitle = {Ice recrystallisation inhibiting polymer nano-objects via saline-tolerant polymerisation-induced self-assembly},\n\tissn = {2051-6355},\n\turl = {https://pubs.rsc.org/en/content/articlelanding/2020/mh/d0mh00354a},\n\tdoi = {10.1039/D0MH00354A},\n\tabstract = {Chemical tools to modulate ice formation/growth have great (bio)technological value, with ice binding/antifreeze proteins being exciting targets for biomimetic materials. Here we introduce polymer nanomaterials that are potent inhibitors of ice recrystallisation using polymerisation-induced self-assembly (PISA), employing a poly(vinyl alcohol) graft macromolecular chain transfer agent (macro-CTA). Crucially, engineering the core-forming block with diacetone acrylamide enabled PISA to be conducted in saline, whereas poly(2-hydroxypropyl methacrylate) cores led to coagulation. The most active particles inhibited ice growth as low as 0.5 mg mL-1, and were more active than the PVA stabiliser block alone, showing that the dense packing of this nanoparticle format enhanced activity. This provides a unique route towards colloids capable of modulating ice growth.},\n\tlanguage = {en},\n\turldate = {2020-06-11},\n\tjournal = {Mater. Horiz.},\n\tauthor = {Georgiou, Panagiotis G. and Kontopoulou, Ioanna and Congdon, Thomas R. and Gibson, Matthew I.},\n\tmonth = may,\n\tyear = {2020},\n\tnote = {Publisher: The Royal Society of Chemistry},\n\tfile = {Full Text PDF:/Users/wolf/Zotero/storage/77P2MD8X/Georgiou et al. - 2020 - Ice recrystallisation inhibiting polymer nano-obje.pdf:application/pdf;Snapshot:/Users/wolf/Zotero/storage/T3ITX2JM/d0mh00354a.html:text/html}\n}\n\n\n\n Chemical tools to modulate ice formation/growth have great (bio)technological value, with ice binding/antifreeze proteins being exciting targets for biomimetic materials. Here we introduce polymer nanomaterials that are potent inhibitors of ice recrystallisation using polymerisation-induced self-assembly (PISA), employing a poly(vinyl alcohol) graft macromolecular chain transfer agent (macro-CTA). Crucially, engineering the core-forming block with diacetone acrylamide enabled PISA to be conducted in saline, whereas poly(2-hydroxypropyl methacrylate) cores led to coagulation. The most active particles inhibited ice growth as low as 0.5 mg mL-1, and were more active than the PVA stabiliser block alone, showing that the dense packing of this nanoparticle format enhanced activity. This provides a unique route towards colloids capable of modulating ice growth.\n
\n\n\n\n \n\n \n \n \n \n \n \n Cryopreservation of primary cultures of mammalian somatic cells in 96-well plates benefits from control of ice nucleation.\n \n \n \n \n\n\n \n Daily, M. I.; Whale, T. F.; Partanen, R.; Harrison, A. D.; Kilbride, P.; Lamb, S.; Morris, G. J.; Picton, H. M.; and Murray, B. J.\n\n\n \n\n\n\n Cryobiology, 93: 62 – 69. 2020.\n \n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n@article{daily_cryopreservation_2020,\n\ttitle = {Cryopreservation of primary cultures of mammalian somatic cells in 96-well plates benefits from control of ice nucleation},\n\tvolume = {93},\n\tissn = {0011-2240},\n\turl = {http://www.sciencedirect.com/science/article/pii/S0011224019306376},\n\tdoi = {https://doi.org/10.1016/j.cryobiol.2020.02.008},\n\tabstract = {Cryopreservation of mammalian cells has to date typically been conducted in cryovials, but there are applications where cryopreservation of primary cells in multiwell plates would be advantageous. However excessive supercooling in the small volumes of liquid in each well of the multiwell plates is inevitable without intervention and tends to result in high and variable cell mortality. Here, we describe a technique for cryopreservation of adhered primary bovine granulosa cells in 96-well plates by controlled rate freezing using controlled ice nucleation. Inducing ice nucleation at warm supercooled temperatures (less than 5 {\\textdegree}C below the melting point) during cryopreservation using a manual seeding technique significantly improved post-thaw recovery from 29.6\\% (SD = 8.3\\%) where nucleation was left uncontrolled to 57.7\\% (9.3\\%) when averaged over 8 replicate cultures (p {\\textless} 0.001). Detachment of thawed cells was qualitatively observed to be more prevalent in wells which did not have ice nucleation control which suggests cryopreserved cell monolayer detachment may be a consequence of deep supercooling. Using an infra-red thermography technique we showed that many aliquots of cryoprotectant solution in 96-well plates can supercool to temperatures below -20 {\\textdegree}C when nucleation is not controlled, and also that the freezing temperatures observed are highly variable despite stringent attempts to remove contaminants acting as nucleation sites. We conclude that successful cryopreservation of cells in 96-well plates, or any small volume format, requires control of ice nucleation.},\n\tjournal = {Cryobiology},\n\tauthor = {Daily, Martin I. and Whale, Thomas F. and Partanen, Riitta and Harrison, Alexander D. and Kilbride, Peter and Lamb, Stephen and Morris, G. John and Picton, Helen M. and Murray, Benjamin J.},\n\tyear = {2020},\n\tpages = {62 -- 69}\n}\n\n\n\n Cryopreservation of mammalian cells has to date typically been conducted in cryovials, but there are applications where cryopreservation of primary cells in multiwell plates would be advantageous. However excessive supercooling in the small volumes of liquid in each well of the multiwell plates is inevitable without intervention and tends to result in high and variable cell mortality. Here, we describe a technique for cryopreservation of adhered primary bovine granulosa cells in 96-well plates by controlled rate freezing using controlled ice nucleation. Inducing ice nucleation at warm supercooled temperatures (less than 5 °C below the melting point) during cryopreservation using a manual seeding technique significantly improved post-thaw recovery from 29.6% (SD = 8.3%) where nucleation was left uncontrolled to 57.7% (9.3%) when averaged over 8 replicate cultures (p \\textless 0.001). Detachment of thawed cells was qualitatively observed to be more prevalent in wells which did not have ice nucleation control which suggests cryopreserved cell monolayer detachment may be a consequence of deep supercooling. Using an infra-red thermography technique we showed that many aliquots of cryoprotectant solution in 96-well plates can supercool to temperatures below -20 °C when nucleation is not controlled, and also that the freezing temperatures observed are highly variable despite stringent attempts to remove contaminants acting as nucleation sites. We conclude that successful cryopreservation of cells in 96-well plates, or any small volume format, requires control of ice nucleation.\n
\n\n\n\n \n\n \n \n \n \n \n \n Post-Thaw Culture and Measurement of Total Cell Recovery Is Crucial in the Evaluation of New Macromolecular Cryoprotectants.\n \n \n \n \n\n\n \n Murray, K. A.; and Gibson, M. I.\n\n\n \n\n\n\n Biomacromolecules. June 2020.\n \n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n@article{murray_post-thaw_2020,\n\ttitle = {Post-{Thaw} {Culture} and {Measurement} of {Total} {Cell} {Recovery} {Is} {Crucial} in the {Evaluation} of {New} {Macromolecular} {Cryoprotectants}},\n\tissn = {1525-7797, 1526-4602},\n\turl = {https://pubs.acs.org/doi/10.1021/acs.biomac.0c00591},\n\tdoi = {10.1021/acs.biomac.0c00591},\n\tabstract = {The storage and transport of cells is a fundamental technology which underpins cell biology, biomaterials research, and emerging cell-based therapies. Inspired by antifreeze and icebinding proteins in extremophiles, macromolecular (polymer) cryoprotectants are emerging as exciting biomaterials to enable the reduction and/or replacement of conventional cryoprotective agents such as DMSO. Here, we critically study post-thaw cellular outcomes upon addition of macromolecular cryoprotectants to provide unambiguous evidence that post-thaw culturing time and a mixture of assays are essential to claim a positive outcome. In particular, we observe that only measuring the viability of recovered cells gives false positives, even with non-cryoprotective polymers. Several systems gave apparently high viability but very low total cell recovery, which could be reported as a success but in practical applications would not be useful. Post-thaw culture time is also shown to be crucial to enable apoptosis to set in. Using this approach we demonstrate that polyampholytes (a rapidly emerging class of cryoprotectants) improve post-thaw outcomes across both measures, compared to poly(ethylene glycol), which can give false positives when only viability and short post-thaw time scales are considered. This work will help guide the discovery of new macromolecular cryoprotectants and ensure materials which only give positive results under limited outcomes can be quickly identified and removed.},\n\tlanguage = {en},\n\turldate = {2020-06-23},\n\tjournal = {Biomacromolecules},\n\tauthor = {Murray, Kathryn A. and Gibson, Matthew I.},\n\tmonth = jun,\n\tyear = {2020},\n\tfile = {Murray and Gibson - 2020 - Post-Thaw Culture and Measurement of Total Cell Re.pdf:/Users/wolf/Zotero/storage/6UVQP6IT/Murray and Gibson - 2020 - Post-Thaw Culture and Measurement of Total Cell Re.pdf:application/pdf}\n}\n\n\n The storage and transport of cells is a fundamental technology which underpins cell biology, biomaterials research, and emerging cell-based therapies. Inspired by antifreeze and icebinding proteins in extremophiles, macromolecular (polymer) cryoprotectants are emerging as exciting biomaterials to enable the reduction and/or replacement of conventional cryoprotective agents such as DMSO. Here, we critically study post-thaw cellular outcomes upon addition of macromolecular cryoprotectants to provide unambiguous evidence that post-thaw culturing time and a mixture of assays are essential to claim a positive outcome. In particular, we observe that only measuring the viability of recovered cells gives false positives, even with non-cryoprotective polymers. Several systems gave apparently high viability but very low total cell recovery, which could be reported as a success but in practical applications would not be useful. Post-thaw culture time is also shown to be crucial to enable apoptosis to set in. Using this approach we demonstrate that polyampholytes (a rapidly emerging class of cryoprotectants) improve post-thaw outcomes across both measures, compared to poly(ethylene glycol), which can give false positives when only viability and short post-thaw time scales are considered. This work will help guide the discovery of new macromolecular cryoprotectants and ensure materials which only give positive results under limited outcomes can be quickly identified and removed.\n
\n\n\n\n
\n\n \n \n 2019\n \n \n (10)\n \n \n
\n \n \n \n
\n \n \n\n \n \n \n \n \n \n Ice is born in low-mobility regions of supercooled liquid water.\n \n \n \n \n\n\n \n Fitzner, M.; Sosso, G. C.; Cox, S. J.; and Michaelides, A.\n\n\n \n\n\n\n Proceedings of the National Academy of Sciences, 116(6): 2009–2014. February 2019.\n \n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n\n@article{fitzner_ice_2019,\n\ttitle = {Ice is born in low-mobility regions of supercooled liquid water},\n\tvolume = {116},\n\tissn = {0027-8424, 1091-6490},\n\turl = {http://www.pnas.org/lookup/doi/10.1073/pnas.1817135116},\n\tdoi = {10.1073/pnas.1817135116},\n\tlanguage = {en},\n\tnumber = {6},\n\turldate = {2019-04-03},\n\tjournal = {Proceedings of the National Academy of Sciences},\n\tauthor = {Fitzner, Martin and Sosso, Gabriele C. and Cox, Stephen J. and Michaelides, Angelos},\n\tmonth = feb,\n\tyear = {2019},\n\tpages = {2009--2014},\n\tfile = {Fitzner et al. - 2019 - Ice is born in low-mobility regions of supercooled.pdf:/Users/wolf/Zotero/storage/PNQQ3VLQ/Fitzner et al. - 2019 - Ice is born in low-mobility regions of supercooled.pdf:application/pdf}\n}\n\n\n\n \n\n \n \n \n \n \n \n Promoting transparency and reproducibility in enhanced molecular simulations.\n \n \n \n \n\n\n \n Bonomi, M.; Bussi, G.; Camilloni, C.; Tribello, G. A.; Baná ̌s, P.; Barducci, A.; Bernetti, M.; Bolhuis, P. G.; Bottaro, S.; Branduardi, D.; Capelli, R.; Carloni, P.; Ceriotti, M.; Cesari, A.; Chen, H.; Chen, W.; Colizzi, F.; De, S.; De La Pierre, M.; Donadio, D.; Drobot, V.; Ensing, B.; Ferguson, A. L.; Filizola, M.; Fraser, J. S.; Fu, H.; Gasparotto, P.; Gervasio, F. L.; Giberti, F.; Gil-Ley, A.; Giorgino, T.; Heller, G. T.; Hocky, G. M.; Iannuzzi, M.; Invernizzi, M.; Jelfs, K. E.; Jussupow, A.; Kirilin, E.; Laio, A.; Limongelli, V.; Lindorff-Larsen, K.; Löhr, T.; Marinelli, F.; Martin-Samos, L.; Masetti, M.; Meyer, R.; Michaelides, A.; Molteni, C.; Morishita, T.; Nava, M.; Paissoni, C.; Papaleo, E.; Parrinello, M.; Pfaendtner, J.; Piaggi, P.; Piccini, G.; Pietropaolo, A.; Pietrucci, F.; Pipolo, S.; Provasi, D.; Quigley, D.; Raiteri, P.; Raniolo, S.; Rydzewski, J.; Salvalaglio, M.; Sosso, G. C.; Spiwok, V.; ̌Sponer, J.; Swenson, D. W. H.; Tiwary, P.; Valsson, O.; Vendruscolo, M.; Voth, G. A.; White, A.; and The PLUMED consortium\n\n\n \n\n\n\n Nature Methods, 16(8): 670–673. August 2019.\n \n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n@article{bonomi_promoting_2019,\n\ttitle = {Promoting transparency and reproducibility in enhanced molecular simulations},\n\tvolume = {16},\n\tissn = {1548-7105},\n\turl = {https://doi.org/10.1038/s41592-019-0506-8},\n\tdoi = {10.1038/s41592-019-0506-8},\n\tabstract = {The PLUMED consortium unifies developers and contributors to PLUMED, an open-source library for enhanced-sampling, free-energy calculations and the analysis of molecular dynamics simulations. Here, we outline our efforts to promote transparency and reproducibility by disseminating protocols for enhanced-sampling molecular simulations.},\n\tnumber = {8},\n\tjournal = {Nature Methods},\n\tauthor = {Bonomi, Massimiliano and Bussi, Giovanni and Camilloni, Carlo and Tribello, Gareth A. and Ban{\\'a}{\\v s}, Pavel and Barducci, Alessandro and Bernetti, Mattia and Bolhuis, Peter G. and Bottaro, Sandro and Branduardi, Davide and Capelli, Riccardo and Carloni, Paolo and Ceriotti, Michele and Cesari, Andrea and Chen, Haochuan and Chen, Wei and Colizzi, Francesco and De, Sandip and De La Pierre, Marco and Donadio, Davide and Drobot, Viktor and Ensing, Bernd and Ferguson, Andrew L. and Filizola, Marta and Fraser, James S. and Fu, Haohao and Gasparotto, Piero and Gervasio, Francesco Luigi and Giberti, Federico and Gil-Ley, Alejandro and Giorgino, Toni and Heller, Gabriella T. and Hocky, Glen M. and Iannuzzi, Marcella and Invernizzi, Michele and Jelfs, Kim E. and Jussupow, Alexander and Kirilin, Evgeny and Laio, Alessandro and Limongelli, Vittorio and Lindorff-Larsen, Kresten and L{\\"o}hr, Thomas and Marinelli, Fabrizio and Martin-Samos, Layla and Masetti, Matteo and Meyer, Ralf and Michaelides, Angelos and Molteni, Carla and Morishita, Tetsuya and Nava, Marco and Paissoni, Cristina and Papaleo, Elena and Parrinello, Michele and Pfaendtner, Jim and Piaggi, Pablo and Piccini, GiovanniMaria and Pietropaolo, Adriana and Pietrucci, Fabio and Pipolo, Silvio and Provasi, Davide and Quigley, David and Raiteri, Paolo and Raniolo, Stefano and Rydzewski, Jakub and Salvalaglio, Matteo and Sosso, Gabriele Cesare and Spiwok, Vojt{\\v e}ch and {\\v S}poner, Ji{\\v r}{\\'i} and Swenson, David W. H. and Tiwary, Pratyush and Valsson, Omar and Vendruscolo, Michele and Voth, Gregory A. and White, Andrew and {The PLUMED consortium}},\n\tmonth = aug,\n\tyear = {2019},\n\tpages = {670--673}\n}\n\n\n\n The PLUMED consortium unifies developers and contributors to PLUMED, an open-source library for enhanced-sampling, free-energy calculations and the analysis of molecular dynamics simulations. Here, we outline our efforts to promote transparency and reproducibility by disseminating protocols for enhanced-sampling molecular simulations.\n
\n\n\n\n \n\n \n \n \n \n \n \n Enhancement of Macromolecular Ice Recrystallization Inhibition Activity by Exploiting Depletion Forces.\n \n \n \n \n\n\n \n Ishibe, T.; Congdon, T.; Stubbs, C.; Hasan, M.; Sosso, G. C.; and Gibson, M. I.\n\n\n \n\n\n\n ACS Macro Lett., 8(8): 1063–1067. August 2019.\n \n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n@article{ishibe_enhancement_2019,\n\ttitle = {Enhancement of {Macromolecular} {Ice} {Recrystallization} {Inhibition} {Activity} by {Exploiting} {Depletion} {Forces}},\n\tvolume = {8},\n\turl = {https://doi.org/10.1021/acsmacrolett.9b00386},\n\tdoi = {10.1021/acsmacrolett.9b00386},\n\tabstract = {Antifreeze (glyco) proteins (AF(G)Ps) are potent inhibitors of ice recrystallization and may have biotechnological applications. The most potent AF(G)Ps function at concentrations a thousand times lower than synthetic mimics such as poly(vinyl alcohol), PVA. Here, we demonstrate that PVA{\\textquoteright}s ice recrystallization activity can be rescued at concentrations where it does not normally function, by the addition of noninteracting polymeric depletants, due to PVA forming colloids in the concentrated saline environment present between ice crystals. These depletants shift the equilibrium toward ice binding and, hence, enable PVA to inhibit ice growth at lower concentrations. Using theory and experiments, we show this effect requires polymeric depletants, not small molecules, to enhance activity. These results increase our understanding of how to design new ice growth inhibitors, but also offer opportunities to enhance activity by exploiting depletion forces, without re-engineering ice-binding materials. It also shows that when screening for IRI activity that polymer contaminants in buffers may give rise to false positive results.},\n\tnumber = {8},\n\turldate = {2020-02-06},\n\tjournal = {ACS Macro Lett.},\n\tauthor = {Ishibe, Toru and Congdon, Thomas and Stubbs, Christopher and Hasan, Muhammad and Sosso, Gabriele C. and Gibson, Matthew I.},\n\tmonth = aug,\n\tyear = {2019},\n\tpages = {1063--1067},\n\tfile = {ACS Full Text Snapshot:/Users/wolf/Zotero/storage/PU8JSG2C/acsmacrolett.html:text/html;Full Text PDF:/Users/wolf/Zotero/storage/3S2X3PBB/Ishibe et al. - 2019 - Enhancement of Macromolecular Ice Recrystallizatio.pdf:application/pdf}\n}\n\n\n\n Antifreeze (glyco) proteins (AF(G)Ps) are potent inhibitors of ice recrystallization and may have biotechnological applications. The most potent AF(G)Ps function at concentrations a thousand times lower than synthetic mimics such as poly(vinyl alcohol), PVA. Here, we demonstrate that PVA\\textquoterights ice recrystallization activity can be rescued at concentrations where it does not normally function, by the addition of noninteracting polymeric depletants, due to PVA forming colloids in the concentrated saline environment present between ice crystals. These depletants shift the equilibrium toward ice binding and, hence, enable PVA to inhibit ice growth at lower concentrations. Using theory and experiments, we show this effect requires polymeric depletants, not small molecules, to enhance activity. These results increase our understanding of how to design new ice growth inhibitors, but also offer opportunities to enhance activity by exploiting depletion forces, without re-engineering ice-binding materials. It also shows that when screening for IRI activity that polymer contaminants in buffers may give rise to false positive results.\n
\n\n\n\n \n\n \n \n \n \n \n \n Photo-polymerisation and study of the ice recrystallisation inhibition of hydrophobically modified poly(vinyl pyrrolidone) co-polymers.\n \n \n \n \n\n\n \n Stubbs, C.; Congdon, T. R; and Gibson, M. I.\n\n\n \n\n\n\n European Polymer Journal, 110: 330–336. January 2019.\n \n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n\n\n\n\n
\n\n\n@article{stubbs_photo-polymerisation_2019,\n\ttitle = {Photo-polymerisation and study of the ice recrystallisation inhibition of hydrophobically modified poly(vinyl pyrrolidone) co-polymers},\n\tvolume = {110},\n\tissn = {0014-3057},\n\turl = {http://www.sciencedirect.com/science/article/pii/S0014305718318676},\n\tdoi = {10.1016/j.eurpolymj.2018.11.047},\n\tabstract = {Antifreeze, ice binding and ice nucleating proteins modulate the formation and growth of ice in biological systems, enabling extremophiles to survive in sub-zero temperatures. A common feature is their rigidity, and segregated hydrophobic and hydrophilic domains. It has been demonstrated that increased hydrophobicity in rigid, facially amphipathic, synthetic polymers enhances ice recrystallisation inhibition (IRI) activity, but has not been evaluated in flexible systems. Here photochemical RAFT/MADIX polymerisation is used to obtain well-defined poly(N-vinyl pyrrolidone), PVP, copolymers to probe the impact of hydrophobicity on ice recrystallisation inhibition in a fully flexible polymer system, to increase the understanding on how to mimic antifreeze proteins. It is observed that PVP homopolymers have only very weak, molecular weight dependent, IRI and that hydrophobic co-monomers give very modest changes in IRI, demonstrating that the spacial segregation of {\\textquoteleft}philicities{\\textquoteright} is crucial, and not just the overall hydrophobic content of the polymer. These results will help design the next generation of IRI active polymers for cryopreservation applications as well as aid our understanding of how biomacromolecules can inhibit ice growth.},\n\tlanguage = {en},\n\turldate = {2020-06-11},\n\tjournal = {European Polymer Journal},\n\tauthor = {Stubbs, Christopher and Congdon, Thomas R and Gibson, Matthew I.},\n\tmonth = jan,\n\tyear = {2019},\n\tkeywords = {Polymers, Ice growth inhibition, Photo chemistry, Post-polymerisation modification},\n\tpages = {330--336},\n\tfile = {ScienceDirect Snapshot:/Users/wolf/Zotero/storage/ET8BAQPE/S0014305718318676.html:text/html}\n}\n\n\n\n Antifreeze, ice binding and ice nucleating proteins modulate the formation and growth of ice in biological systems, enabling extremophiles to survive in sub-zero temperatures. A common feature is their rigidity, and segregated hydrophobic and hydrophilic domains. It has been demonstrated that increased hydrophobicity in rigid, facially amphipathic, synthetic polymers enhances ice recrystallisation inhibition (IRI) activity, but has not been evaluated in flexible systems. Here photochemical RAFT/MADIX polymerisation is used to obtain well-defined poly(N-vinyl pyrrolidone), PVP, copolymers to probe the impact of hydrophobicity on ice recrystallisation inhibition in a fully flexible polymer system, to increase the understanding on how to mimic antifreeze proteins. It is observed that PVP homopolymers have only very weak, molecular weight dependent, IRI and that hydrophobic co-monomers give very modest changes in IRI, demonstrating that the spacial segregation of \\textquoteleftphilicities\\textquoteright is crucial, and not just the overall hydrophobic content of the polymer. These results will help design the next generation of IRI active polymers for cryopreservation applications as well as aid our understanding of how biomacromolecules can inhibit ice growth.\n
\n\n\n\n \n\n \n \n \n \n \n \n Ice-recrystallization inhibiting polymers protect proteins against freeze-stress and enable glycerol-free cryostorage.\n \n \n \n \n\n\n \n Mitchell, D. E.; Fayter, A. E. R.; Deller, R. C.; Hasan, M.; Gutierrez-Marcos, J.; and Gibson, M. I.\n\n\n \n\n\n\n Mater. Horiz., 6(2): 364–368. February 2019.\n Publisher: The Royal Society of Chemistry\n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n@article{mitchell_ice-recrystallization_2019,\n\ttitle = {Ice-recrystallization inhibiting polymers protect proteins against freeze-stress and enable glycerol-free cryostorage},\n\tvolume = {6},\n\tissn = {2051-6355},\n\turl = {https://pubs.rsc.org/en/content/articlelanding/2019/mh/c8mh00727f},\n\tdoi = {10.1039/C8MH00727F},\n\tabstract = {Proteins are ubiquitous in molecular biotechnology, biotechnology and as therapeutics, but there are significant challenges in their storage and distribution, with freezing often required. This is traditionally achieved by the addition of cryoprotective agents such as glycerol (or trehalose) or covalent modification of mutated proteins with cryoprotectants. Here, ice recrystallization inhibiting polymers, inspired by antifreeze proteins, are used synergistically with poly(ethylene glycol) as an alternative to glycerol. The primary mechanism of action appears to be preventing irreversible aggregation due to ice growth. The polymer formulation is successfully used to cryopreserve a range of important proteins including insulin, Taq DNA polymerase and an IgG antibody. The polymers do not require covalent conjugation, nor modification of the protein and are already used in a wide range of biomedical applications, which will facilitate translation to a range of biologics.},\n\tlanguage = {en},\n\tnumber = {2},\n\turldate = {2020-06-11},\n\tjournal = {Mater. Horiz.},\n\tauthor = {Mitchell, Daniel E. and Fayter, Alice E. R. and Deller, Robert C. and Hasan, Muhammad and Gutierrez-Marcos, Jose and Gibson, Matthew I.},\n\tmonth = feb,\n\tyear = {2019},\n\tnote = {Publisher: The Royal Society of Chemistry},\n\tpages = {364--368},\n\tfile = {Full Text PDF:/Users/wolf/Zotero/storage/IDM9DE6P/Mitchell et al. - 2019 - Ice-recrystallization inhibiting polymers protect .pdf:application/pdf;Snapshot:/Users/wolf/Zotero/storage/MUUNNDWT/C8MH00727F.html:text/html}\n}\n\n\n\n Proteins are ubiquitous in molecular biotechnology, biotechnology and as therapeutics, but there are significant challenges in their storage and distribution, with freezing often required. This is traditionally achieved by the addition of cryoprotective agents such as glycerol (or trehalose) or covalent modification of mutated proteins with cryoprotectants. Here, ice recrystallization inhibiting polymers, inspired by antifreeze proteins, are used synergistically with poly(ethylene glycol) as an alternative to glycerol. The primary mechanism of action appears to be preventing irreversible aggregation due to ice growth. The polymer formulation is successfully used to cryopreserve a range of important proteins including insulin, Taq DNA polymerase and an IgG antibody. The polymers do not require covalent conjugation, nor modification of the protein and are already used in a wide range of biomedical applications, which will facilitate translation to a range of biologics.\n
\n\n\n\n \n\n \n \n \n \n \n \n Site-specific conjugation of antifreeze proteins onto polymer-stabilized nanoparticles.\n \n \n \n \n\n\n \n Wilkins, L. E.; Hasan, M.; Fayter, A. E. R.; Biggs, C.; Walker, M.; and Gibson, M. I.\n\n\n \n\n\n\n Polym. Chem., 10(23): 2986–2990. June 2019.\n Publisher: The Royal Society of Chemistry\n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n@article{wilkins_site-specific_2019,\n\ttitle = {Site-specific conjugation of antifreeze proteins onto polymer-stabilized nanoparticles},\n\tvolume = {10},\n\tissn = {1759-9962},\n\turl = {https://pubs.rsc.org/en/content/articlelanding/2019/py/c8py01719k},\n\tdoi = {10.1039/C8PY01719K},\n\tabstract = {Antifreeze proteins (AFPs) have many potential applications, ranging from cryobiology to aerospace, if they can be incorporated into materials. Here, a range of engineered AFP mutants were prepared and site-specifically conjugated onto RAFT polymer-stabilized gold nanoparticles to generate new hybrid multivalent ice growth inhibitors. Only the SNAP-tagged AFPs lead to potent {\\textquoteleft}antifreeze{\\textquoteright} active nanomaterials with His-Tag capture resulting in no activity, showing the mode of conjugation is essential. This versatile strategy will enable the development of multivalent AFPs for translational and fundamental studies.},\n\tlanguage = {en},\n\tnumber = {23},\n\turldate = {2020-06-11},\n\tjournal = {Polym. Chem.},\n\tauthor = {Wilkins, Laura E. and Hasan, Muhammad and Fayter, Alice E. R. and Biggs, Caroline and Walker, Marc and Gibson, Matthew I.},\n\tmonth = jun,\n\tyear = {2019},\n\tnote = {Publisher: The Royal Society of Chemistry},\n\tpages = {2986--2990},\n\tfile = {Full Text PDF:/Users/wolf/Zotero/storage/QMZI4BMP/Wilkins et al. - 2019 - Site-specific conjugation of antifreeze proteins o.pdf:application/pdf;Snapshot:/Users/wolf/Zotero/storage/3JPSA2JC/c8py01719k.html:text/html}\n}\n\n\n\n Antifreeze proteins (AFPs) have many potential applications, ranging from cryobiology to aerospace, if they can be incorporated into materials. Here, a range of engineered AFP mutants were prepared and site-specifically conjugated onto RAFT polymer-stabilized gold nanoparticles to generate new hybrid multivalent ice growth inhibitors. Only the SNAP-tagged AFPs lead to potent \\textquoteleftantifreeze\\textquoteright active nanomaterials with His-Tag capture resulting in no activity, showing the mode of conjugation is essential. This versatile strategy will enable the development of multivalent AFPs for translational and fundamental studies.\n
\n\n\n\n \n\n \n \n \n \n \n \n Mimicking the Ice Recrystallization Activity of Biological Antifreezes. When is a New Polymer “Active”?.\n \n \n \n \n\n\n \n Biggs, C. I.; Stubbs, C.; Graham, B.; Fayter, A. E. R.; Hasan, M.; and Gibson, M. I.\n\n\n \n\n\n\n Macromolecular Bioscience, 19(7): 1900082. 2019.\n _eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1002/mabi.201900082\n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n \n \n \n \n \n \n \n \n \n \n\n\n\n\n
\n\n\n@article{biggs_mimicking_2019,\n\ttitle = {Mimicking the {Ice} {Recrystallization} {Activity} of {Biological} {Antifreezes}. {When} is a {New} {Polymer} {\\textquotedblleft}{Active}{\\textquotedblright}?},\n\tvolume = {19},\n\tcopyright = {{\\textcopyright} 2019 The Authors. Published by WILEY-VCH Verlag GmbH \\& Co. KGaA, Weinheim.},\n\tissn = {1616-5195},\n\turl = {https://onlinelibrary.wiley.com/doi/abs/10.1002/mabi.201900082},\n\tdoi = {10.1002/mabi.201900082},\n\tabstract = {Antifreeze proteins and ice-binding proteins have been discovered in a diverse range of extremophiles and have the ability to modulate the growth and formation of ice crystals. Considering the importance of cryoscience across transport, biomedicine, and climate science, there is significant interest in developing synthetic macromolecular mimics of antifreeze proteins, in particular to reproduce their property of ice recrystallization inhibition (IRI). This activity is a continuum rather than an {\\textquotedblleft}on/off{\\textquotedblright} property and there may be multiple molecular mechanisms which give rise to differences in this observable property; the limiting concentrations for ice growth vary by more than a thousand between an antifreeze glycoprotein and poly(vinyl alcohol), for example. The aim of this article is to provide a concise comparison of a range of natural and synthetic materials that are known to have IRI, thus providing a guide to see if a new synthetic mimic is active or not, including emerging materials which are comparatively weak compared to antifreeze proteins, but may have technological importance. The link between activity and the mechanisms involving either ice binding or amphiphilicity is discussed and known materials assigned into classes based on this.},\n\tlanguage = {en},\n\tnumber = {7},\n\turldate = {2020-06-11},\n\tjournal = {Macromolecular Bioscience},\n\tauthor = {Biggs, Caroline I. and Stubbs, Christopher and Graham, Ben and Fayter, Alice E. R. and Hasan, Muhammad and Gibson, Matthew I.},\n\tyear = {2019},\n\tnote = {\\_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1002/mabi.201900082},\n\tkeywords = {cryopreservation, antifreeze proteins, ice recrystallization, polymers, biomaterials},\n\tpages = {1900082},\n\tfile = {Full Text PDF:/Users/wolf/Zotero/storage/ZINWVHK6/Biggs et al. - 2019 - Mimicking the Ice Recrystallization Activity of Bi.pdf:application/pdf;Snapshot:/Users/wolf/Zotero/storage/7YDUGX5K/mabi.html:text/html}\n}\n\n\n\n Antifreeze proteins and ice-binding proteins have been discovered in a diverse range of extremophiles and have the ability to modulate the growth and formation of ice crystals. Considering the importance of cryoscience across transport, biomedicine, and climate science, there is significant interest in developing synthetic macromolecular mimics of antifreeze proteins, in particular to reproduce their property of ice recrystallization inhibition (IRI). This activity is a continuum rather than an “on/off” property and there may be multiple molecular mechanisms which give rise to differences in this observable property; the limiting concentrations for ice growth vary by more than a thousand between an antifreeze glycoprotein and poly(vinyl alcohol), for example. The aim of this article is to provide a concise comparison of a range of natural and synthetic materials that are known to have IRI, thus providing a guide to see if a new synthetic mimic is active or not, including emerging materials which are comparatively weak compared to antifreeze proteins, but may have technological importance. The link between activity and the mechanisms involving either ice binding or amphiphilicity is discussed and known materials assigned into classes based on this.\n
\n\n\n\n \n\n \n \n \n \n \n \n Synthetically Scalable Poly(ampholyte) Which Dramatically Enhances Cellular Cryopreservation.\n \n \n \n \n\n\n \n Bailey, T. L.; Stubbs, C.; Murray, K.; Tomás, R. M. F.; Otten, L.; and Gibson, M. I.\n\n\n \n\n\n\n Biomacromolecules, 20(8): 3104–3114. August 2019.\n Publisher: American Chemical Society\n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n@article{bailey_synthetically_2019,\n\ttitle = {Synthetically {Scalable} {Poly}(ampholyte) {Which} {Dramatically} {Enhances} {Cellular} {Cryopreservation}},\n\tvolume = {20},\n\tissn = {1525-7797},\n\turl = {https://doi.org/10.1021/acs.biomac.9b00681},\n\tdoi = {10.1021/acs.biomac.9b00681},\n\tabstract = {The storage and transport of frozen cells underpin the emerging/existing cell-based therapies and are used in every biomedical research lab globally. The current gold-standard cryoprotectant dimethyl sulfoxide (DMSO) does not give quantitative cell recovery in suspension or in two-dimensional (2D) or three-dimensional (3D) cell models, and the solvent and cell debris must be removed prior to application/transfusion. There is a real need to improve this 50-year-old method to underpin emerging regenerative and cell-based therapies. Here, we introduce a potent and synthetically scalable polymeric cryopreservation enhancer which is easily obtained in a single step from a low cost and biocompatible precursor, poly(methyl vinyl ether-alt-maleic anhydride). This poly(ampholyte) enables post-thaw recoveries of up to 88\\% for a 2D cell monolayer model compared to just 24\\% using conventional DMSO cryopreservation. The poly(ampholyte) also enables reduction of [DMSO] from 10 wt \\% to just 2.5 wt \\% in suspension cryopreservation, which can reduce the negative side effects and speed up post-thaw processing. After thawing, the cells have reduced membrane damage and faster growth rates compared to those without the polymer. The polymer appears to function by a unique extracellular mechanism by stabilization of the cell membrane, rather than by modulation of ice formation and growth. This new macromolecular cryoprotectant will find applications across basic and translational biomedical science and may improve the cold chain for cell-based therapies.},\n\tnumber = {8},\n\turldate = {2020-06-11},\n\tjournal = {Biomacromolecules},\n\tauthor = {Bailey, Trisha L. and Stubbs, Christopher and Murray, Kathryn and Tom{\\'a}s, Ruben M. F. and Otten, Lucienne and Gibson, Matthew I.},\n\tmonth = aug,\n\tyear = {2019},\n\tnote = {Publisher: American Chemical Society},\n\tpages = {3104--3114},\n\tfile = {ACS Full Text Snapshot:/Users/wolf/Zotero/storage/DDATPSLJ/acs.biomac.html:text/html;Full Text PDF:/Users/wolf/Zotero/storage/UCPBWDE4/Bailey et al. - 2019 - Synthetically Scalable Poly(ampholyte) Which Drama.pdf:application/pdf}\n}\n\n\n\n The storage and transport of frozen cells underpin the emerging/existing cell-based therapies and are used in every biomedical research lab globally. The current gold-standard cryoprotectant dimethyl sulfoxide (DMSO) does not give quantitative cell recovery in suspension or in two-dimensional (2D) or three-dimensional (3D) cell models, and the solvent and cell debris must be removed prior to application/transfusion. There is a real need to improve this 50-year-old method to underpin emerging regenerative and cell-based therapies. Here, we introduce a potent and synthetically scalable polymeric cryopreservation enhancer which is easily obtained in a single step from a low cost and biocompatible precursor, poly(methyl vinyl ether-alt-maleic anhydride). This poly(ampholyte) enables post-thaw recoveries of up to 88% for a 2D cell monolayer model compared to just 24% using conventional DMSO cryopreservation. The poly(ampholyte) also enables reduction of [DMSO] from 10 wt % to just 2.5 wt % in suspension cryopreservation, which can reduce the negative side effects and speed up post-thaw processing. After thawing, the cells have reduced membrane damage and faster growth rates compared to those without the polymer. The polymer appears to function by a unique extracellular mechanism by stabilization of the cell membrane, rather than by modulation of ice formation and growth. This new macromolecular cryoprotectant will find applications across basic and translational biomedical science and may improve the cold chain for cell-based therapies.\n
\n\n\n\n \n\n \n \n \n \n \n \n Extracellular Antifreeze Protein Significantly Enhances the Cryopreservation of Cell Monolayers.\n \n \n \n \n\n\n \n Tomás, R. M. F.; Bailey, T. L.; Hasan, M.; and Gibson, M. I.\n\n\n \n\n\n\n Biomacromolecules, 20(10): 3864–3872. October 2019.\n Publisher: American Chemical Society\n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n@article{tomas_extracellular_2019,\n\ttitle = {Extracellular {Antifreeze} {Protein} {Significantly} {Enhances} the {Cryopreservation} of {Cell} {Monolayers}},\n\tvolume = {20},\n\tissn = {1525-7797},\n\turl = {https://doi.org/10.1021/acs.biomac.9b00951},\n\tdoi = {10.1021/acs.biomac.9b00951},\n\tabstract = {The cryopreservation of cells underpins many areas of biotechnology, healthcare, and fundamental science by enabling the banking and distribution of cells. Cryoprotectants are essential to prevent cold-induced damage. Here, we demonstrate that extracellular localization of antifreeze proteins can significantly enhance post-thaw recovery of mammalian cell monolayers cryopreserved using dimethyl sulfoxide, whereas they show less benefit in suspension cryopreservation. A type III antifreeze protein (AFPIII) was used as the macromolecular ice recrystallization inhibitor and its intra/extracellular locations were controlled by using Pep-1, a cell-penetrating peptide. Flow cytometry and confocal microscopy confirmed successful delivery of AFPIII. The presence of extracellular AFPIII dramatically increased post-thaw recovery in a challenging 2-D cell monolayer system using just 0.8 mg{\\textperiodcentered}mL{\\textendash}1, from 25\\% to over 60\\%, whereas intracellularly delivered AFPIII showed less benefit. Interestingly, the antifreeze protein was less effective when used in suspension cryopreservation of the same cells, suggesting that the cryopreservation format is also crucial. These observations show that, in the discovery of macromolecular cryoprotectants, intracellular delivery of ice recrystallization inhibitors may not be a significant requirement under {\\textquotedblleft}slow freezing{\\textquotedblright} conditions, which will help guide the design of new biomaterials, in particular, for cell storage.},\n\tnumber = {10},\n\turldate = {2020-06-11},\n\tjournal = {Biomacromolecules},\n\tauthor = {Tom{\\'a}s, Ruben M. F. and Bailey, Trisha L. and Hasan, Muhammad and Gibson, Matthew I.},\n\tmonth = oct,\n\tyear = {2019},\n\tnote = {Publisher: American Chemical Society},\n\tpages = {3864--3872},\n\tfile = {ACS Full Text Snapshot:/Users/wolf/Zotero/storage/SUSL7WLV/acs.biomac.html:text/html;Full Text PDF:/Users/wolf/Zotero/storage/3MTXZ8FR/Tom{\\'a}s et al. - 2019 - Extracellular Antifreeze Protein Significantly Enh.pdf:application/pdf}\n}\n\n\n\n The cryopreservation of cells underpins many areas of biotechnology, healthcare, and fundamental science by enabling the banking and distribution of cells. Cryoprotectants are essential to prevent cold-induced damage. Here, we demonstrate that extracellular localization of antifreeze proteins can significantly enhance post-thaw recovery of mammalian cell monolayers cryopreserved using dimethyl sulfoxide, whereas they show less benefit in suspension cryopreservation. A type III antifreeze protein (AFPIII) was used as the macromolecular ice recrystallization inhibitor and its intra/extracellular locations were controlled by using Pep-1, a cell-penetrating peptide. Flow cytometry and confocal microscopy confirmed successful delivery of AFPIII. The presence of extracellular AFPIII dramatically increased post-thaw recovery in a challenging 2-D cell monolayer system using just 0.8 mg˙mL–1, from 25% to over 60%, whereas intracellularly delivered AFPIII showed less benefit. Interestingly, the antifreeze protein was less effective when used in suspension cryopreservation of the same cells, suggesting that the cryopreservation format is also crucial. These observations show that, in the discovery of macromolecular cryoprotectants, intracellular delivery of ice recrystallization inhibitors may not be a significant requirement under “slow freezing” conditions, which will help guide the design of new biomaterials, in particular, for cell storage.\n
\n\n\n\n \n\n \n \n \n \n \n \n Synthesis of Anthracene Conjugates of Truncated Antifreeze Protein Sequences: Effect of the End Group and Photocontrolled Dimerization on Ice Recrystallization Inhibition Activity.\n \n \n \n \n\n\n \n Graham, B.; Fayter, A. E. R.; and Gibson, M. I.\n\n\n \n\n\n\n Biomacromolecules, 20(12): 4611–4621. December 2019.\n Publisher: American Chemical Society\n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n@article{graham_synthesis_2019,\n\ttitle = {Synthesis of {Anthracene} {Conjugates} of {Truncated} {Antifreeze} {Protein} {Sequences}: {Effect} of the {End} {Group} and {Photocontrolled} {Dimerization} on {Ice} {Recrystallization} {Inhibition} {Activity}},\n\tvolume = {20},\n\tissn = {1525-7797},\n\tshorttitle = {Synthesis of {Anthracene} {Conjugates} of {Truncated} {Antifreeze} {Protein} {Sequences}},\n\turl = {https://doi.org/10.1021/acs.biomac.9b01538},\n\tdoi = {10.1021/acs.biomac.9b01538},\n\tabstract = {Biomacromolecular antifreezes distinguish ice from water, function by binding to specific planes of ice, and could have many applications from cryobiology to aerospace where ice is a problem. In biology, antifreeze protein (AFP) activity is regulated by protein expression levels via temperature and light-regulated expression systems, but in the laboratory (or applications), the antifreeze activity is {\\textquotedblleft}always on{\\textquotedblright} without any spatial or temporal control, and hence methods to enable this switching represent an exciting synthetic challenge. Introduction of an abiotic functionality into short peptides (e.g., from solid-phase synthesis) to enable switching is also desirable rather than on full-length recombinant proteins. Here, truncated peptide sequences based on the consensus repeat sequence from type-I AFPs (TAANAAAAAAA) were conjugated to an anthracene unit to explore their photocontrolled dimerization. Optimization of the synthesis to ensure solubility of the hydrophobic peptide included the addition of a dilysine solubilizing linker. It was shown that UV-light exposure triggered reversible dimerization of the AFP sequence, leading to an increase in molecular weight. Assessment of the ice recrystallization inhibition activity of the peptides before and after dimerization revealed only small effects on activity. However, it is reported here for the first time that addition of the anthracene unit to a 22-amino-acid truncated peptide significantly enhanced ice recrystallization inhibition compared to the free peptide, suggesting an accessible synthetic route to allow AFP activity using shorter, synthetically accessible peptides with a photoreactive functionality.},\n\tnumber = {12},\n\turldate = {2020-06-11},\n\tjournal = {Biomacromolecules},\n\tauthor = {Graham, Ben and Fayter, Alice E. R. and Gibson, Matthew I.},\n\tmonth = dec,\n\tyear = {2019},\n\tnote = {Publisher: American Chemical Society},\n\tpages = {4611--4621}\n}\n\n\n\n Biomacromolecular antifreezes distinguish ice from water, function by binding to specific planes of ice, and could have many applications from cryobiology to aerospace where ice is a problem. In biology, antifreeze protein (AFP) activity is regulated by protein expression levels via temperature and light-regulated expression systems, but in the laboratory (or applications), the antifreeze activity is “always on” without any spatial or temporal control, and hence methods to enable this switching represent an exciting synthetic challenge. Introduction of an abiotic functionality into short peptides (e.g., from solid-phase synthesis) to enable switching is also desirable rather than on full-length recombinant proteins. Here, truncated peptide sequences based on the consensus repeat sequence from type-I AFPs (TAANAAAAAAA) were conjugated to an anthracene unit to explore their photocontrolled dimerization. Optimization of the synthesis to ensure solubility of the hydrophobic peptide included the addition of a dilysine solubilizing linker. It was shown that UV-light exposure triggered reversible dimerization of the AFP sequence, leading to an increase in molecular weight. Assessment of the ice recrystallization inhibition activity of the peptides before and after dimerization revealed only small effects on activity. However, it is reported here for the first time that addition of the anthracene unit to a 22-amino-acid truncated peptide significantly enhanced ice recrystallization inhibition compared to the free peptide, suggesting an accessible synthetic route to allow AFP activity using shorter, synthetically accessible peptides with a photoreactive functionality.\n
\n\n\n\n
\n\n \n \n 2018\n \n \n (4)\n \n \n
\n \n \n \n
\n \n \n\n \n \n \n \n \n \n Heterogeneous seeded molecular dynamics as a tool to probe the ice nucleating ability of crystalline surfaces.\n \n \n \n \n\n\n \n Pedevilla, P.; Fitzner, M.; Sosso, G. C.; and Michaelides, A.\n\n\n \n\n\n\n The Journal of Chemical Physics, 149(7): 072327. June 2018.\n \n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n\n@article{pedevilla_heterogeneous_2018,\n\ttitle = {Heterogeneous seeded molecular dynamics as a tool to probe the ice nucleating ability of crystalline surfaces},\n\tvolume = {149},\n\tissn = {0021-9606},\n\turl = {https://aip.scitation.org/doi/10.1063/1.5029336},\n\tdoi = {10.1063/1.5029336},\n\tnumber = {7},\n\turldate = {2018-06-28},\n\tjournal = {The Journal of Chemical Physics},\n\tauthor = {Pedevilla, Philipp and Fitzner, Martin and Sosso, Gabriele C. and Michaelides, Angelos},\n\tmonth = jun,\n\tyear = {2018},\n\tpages = {072327},\n\tfile = {Snapshot:/Users/wolf/Zotero/storage/C2YLY28U/1.html:text/html}\n}\n\n\n\n \n\n \n \n \n \n \n \n Unravelling the origins of ice nucleation on organic crystals.\n \n \n \n \n\n\n \n Sosso, G. C.; Whale, T. F.; Holden, M. A.; Pedevilla, P.; Murray, B. J.; and Michaelides, A.\n\n\n \n\n\n\n Chemical Science, 9(42): 8077–8088. 2018.\n \n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n\n@article{sosso_unravelling_2018,\n\ttitle = {Unravelling the origins of ice nucleation on organic crystals},\n\tvolume = {9},\n\tissn = {2041-6520, 2041-6539},\n\turl = {http://xlink.rsc.org/?DOI=C8SC02753F},\n\tdoi = {10.1039/C8SC02753F},\n\tlanguage = {en},\n\tnumber = {42},\n\turldate = {2019-01-25},\n\tjournal = {Chemical Science},\n\tauthor = {Sosso, Gabriele C. and Whale, Thomas F. and Holden, Mark A. and Pedevilla, Philipp and Murray, Benjamin J. and Michaelides, Angelos},\n\tyear = {2018},\n\tpages = {8077--8088},\n\tfile = {Sosso et al. - 2018 - Unravelling the origins of ice nucleation on organ.pdf:/Users/wolf/Zotero/storage/HPV5AC3R/Sosso et al. - 2018 - Unravelling the origins of ice nucleation on organ.pdf:application/pdf}\n}\n\n\n\n \n\n \n \n \n \n \n \n The enhancement and suppression of immersion mode heterogeneous ice-nucleation by solutes.\n \n \n \n \n\n\n \n Whale, T. F.; Holden, M. A.; Wilson, T. W.; O'Sullivan, D.; and Murray, B. J.\n\n\n \n\n\n\n Chem. Sci., 9(17): 4142–4151. 2018.\n Publisher: The Royal Society of Chemistry\n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n@article{whale_enhancement_2018,\n\ttitle = {The enhancement and suppression of immersion mode heterogeneous ice-nucleation by solutes},\n\tvolume = {9},\n\turl = {http://dx.doi.org/10.1039/C7SC05421A},\n\tdoi = {10.1039/C7SC05421A},\n\tabstract = {Heterogeneous nucleation of ice from aqueous solutions is an important yet poorly understood process in multiple fields, not least the atmospheric sciences where it impacts the formation and properties of clouds. In the atmosphere ice-nucleating particles are usually, if not always, mixed with soluble material. However, the impact of this soluble material on ice nucleation is poorly understood. In the atmospheric community the current paradigm for freezing under mixed phase cloud conditions is that dilute solutions will not influence heterogeneous freezing. By testing combinations of nucleators and solute molecules we have demonstrated that 0.015 M solutions (predicted melting point depression {\\textless}0.1 {\\textdegree}C) of several ammonium salts can cause suspended particles of feldspars and quartz to nucleate ice up to around 3 {\\textdegree}C warmer than they do in pure water. In contrast, dilute solutions of certain alkali metal halides can dramatically depress freezing points for the same nucleators. At 0.015 M, solutes can enhance or deactivate the ice-nucleating ability of a microcline feldspar across a range of more than 10 {\\textdegree}C, which corresponds to a change in active site density of more than a factor of 105. This concentration was chosen for a survey across multiple solutes{\\textendash}nucleant combinations since it had a minimal colligative impact on freezing and is relevant for activating cloud droplets. Other nucleators, for instance a silica gel, are unaffected by these {\\textquoteleft}solute effects{\\textquoteright}, to within experimental uncertainty. This split in response to the presence of solutes indicates that different mechanisms of ice nucleation occur on the different nucleators or that surface modification of relevance to ice nucleation proceeds in different ways for different nucleators. These solute effects on immersion mode ice nucleation may be of importance in the atmosphere as sea salt and ammonium sulphate are common cloud condensation nuclei (CCN) for cloud droplets and are internally mixed with ice-nucleating particles in mixed-phase clouds. In addition, we propose a pathway dependence where activation of CCN at low temperatures might lead to enhanced ice formation relative to pathways where CCN activation occurs at higher temperatures prior to cooling to nucleation temperature.},\n\tnumber = {17},\n\tjournal = {Chem. Sci.},\n\tauthor = {Whale, Thomas F. and Holden, Mark A. and Wilson, Theodore W. and O'Sullivan, Daniel and Murray, Benjamin J.},\n\tyear = {2018},\n\tnote = {Publisher: The Royal Society of Chemistry},\n\tpages = {4142--4151}\n}\n\n\n\n Heterogeneous nucleation of ice from aqueous solutions is an important yet poorly understood process in multiple fields, not least the atmospheric sciences where it impacts the formation and properties of clouds. In the atmosphere ice-nucleating particles are usually, if not always, mixed with soluble material. However, the impact of this soluble material on ice nucleation is poorly understood. In the atmospheric community the current paradigm for freezing under mixed phase cloud conditions is that dilute solutions will not influence heterogeneous freezing. By testing combinations of nucleators and solute molecules we have demonstrated that 0.015 M solutions (predicted melting point depression \\textless0.1 °C) of several ammonium salts can cause suspended particles of feldspars and quartz to nucleate ice up to around 3 °C warmer than they do in pure water. In contrast, dilute solutions of certain alkali metal halides can dramatically depress freezing points for the same nucleators. At 0.015 M, solutes can enhance or deactivate the ice-nucleating ability of a microcline feldspar across a range of more than 10 °C, which corresponds to a change in active site density of more than a factor of 105. This concentration was chosen for a survey across multiple solutes–nucleant combinations since it had a minimal colligative impact on freezing and is relevant for activating cloud droplets. Other nucleators, for instance a silica gel, are unaffected by these \\textquoteleftsolute effects\\textquoteright, to within experimental uncertainty. This split in response to the presence of solutes indicates that different mechanisms of ice nucleation occur on the different nucleators or that surface modification of relevance to ice nucleation proceeds in different ways for different nucleators. These solute effects on immersion mode ice nucleation may be of importance in the atmosphere as sea salt and ammonium sulphate are common cloud condensation nuclei (CCN) for cloud droplets and are internally mixed with ice-nucleating particles in mixed-phase clouds. In addition, we propose a pathway dependence where activation of CCN at low temperatures might lead to enhanced ice formation relative to pathways where CCN activation occurs at higher temperatures prior to cooling to nucleation temperature.\n
\n\n\n\n \n\n \n \n \n \n \n \n An instrument for quantifying heterogeneous ice nucleation in multiwell plates using infrared emissions to detect freezing.\n \n \n \n \n\n\n \n Harrison, A. D.; Whale, T. F.; Rutledge, R.; Lamb, S.; Tarn, M. D.; Porter, G. C. E.; Adams, M. P.; McQuaid, J. B.; Morris, G. J.; and Murray, B. J.\n\n\n \n\n\n\n Atmospheric Measurement Techniques, 11(10): 5629–5641. 2018.\n \n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n\n@article{harrison_instrument_2018,\n\ttitle = {An instrument for quantifying heterogeneous ice nucleation in multiwell plates using infrared emissions to detect freezing},\n\tvolume = {11},\n\turl = {https://www.atmos-meas-tech.net/11/5629/2018/},\n\tdoi = {10.5194/amt-11-5629-2018},\n\tnumber = {10},\n\tjournal = {Atmospheric Measurement Techniques},\n\tauthor = {Harrison, A. D. and Whale, T. F. and Rutledge, R. and Lamb, S. and Tarn, M. D. and Porter, G. C. E. and Adams, M. P. and McQuaid, J. B. and Morris, G. J. and Murray, B. J.},\n\tyear = {2018},\n\tpages = {5629--5641}\n}\n\n\n\n
\n\n \n \n 2017\n \n \n (3)\n \n \n
\n \n \n \n
\n \n \n\n \n \n \n \n \n \n Analyzing and Driving Cluster Formation in Atomistic Simulations.\n \n \n \n \n\n\n \n Tribello, G. A.; Giberti, F.; Sosso, G. C.; Salvalaglio, M.; and Parrinello, M.\n\n\n \n\n\n\n Journal of Chemical Theory and Computation, 13(3): 1317–1327. March 2017.\n \n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n\n@article{tribello_analyzing_2017,\n\ttitle = {Analyzing and {Driving} {Cluster} {Formation} in {Atomistic} {Simulations}},\n\tvolume = {13},\n\tissn = {1549-9618, 1549-9626},\n\turl = {http://pubs.acs.org/doi/10.1021/acs.jctc.6b01073},\n\tdoi = {10.1021/acs.jctc.6b01073},\n\tlanguage = {en},\n\tnumber = {3},\n\turldate = {2018-04-16},\n\tjournal = {Journal of Chemical Theory and Computation},\n\tauthor = {Tribello, Gareth A. and Giberti, Federico and Sosso, Gabriele C. and Salvalaglio, Matteo and Parrinello, Michele},\n\tmonth = mar,\n\tyear = {2017},\n\tpages = {1317--1327}\n}\n\n\n\n \n\n \n \n \n \n \n \n Is High-Density Amorphous Ice Simply a “Derailed” State along the Ice I to Ice IV Pathway?.\n \n \n \n \n\n\n \n Shephard, J. J.; Ling, S.; Sosso, G. C.; Michaelides, A.; Slater, B.; and Salzmann, C. G.\n\n\n \n\n\n\n The Journal of Physical Chemistry Letters, 8(7): 1645–1650. April 2017.\n \n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n\n@article{shephard_is_2017,\n\ttitle = {Is {High}-{Density} {Amorphous} {Ice} {Simply} a {\\textquotedblleft}{Derailed}{\\textquotedblright} {State} along the {Ice} {I} to {Ice} {IV} {Pathway}?},\n\tvolume = {8},\n\tissn = {1948-7185},\n\turl = {http://pubs.acs.org/doi/10.1021/acs.jpclett.7b00492},\n\tdoi = {10.1021/acs.jpclett.7b00492},\n\tlanguage = {en},\n\tnumber = {7},\n\turldate = {2018-04-16},\n\tjournal = {The Journal of Physical Chemistry Letters},\n\tauthor = {Shephard, Jacob J. and Ling, Sanliang and Sosso, Gabriele C. and Michaelides, Angelos and Slater, Ben and Salzmann, Christoph G.},\n\tmonth = apr,\n\tyear = {2017},\n\tpages = {1645--1650}\n}\n\n\n\n \n\n \n \n \n \n \n \n Pre-critical fluctuations and what they disclose about heterogeneous crystal nucleation.\n \n \n \n \n\n\n \n Fitzner, M.; Sosso, G. C.; Pietrucci, F.; Pipolo, S.; and Michaelides, A.\n\n\n \n\n\n\n Nature Communications, 8(1): 2257. December 2017.\n \n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n \n \n abstract \n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n@article{fitzner_pre-critical_2017,\n\ttitle = {Pre-critical fluctuations and what they disclose about heterogeneous crystal nucleation},\n\tvolume = {8},\n\tcopyright = {2017 The Author(s)},\n\tissn = {2041-1723},\n\turl = {https://www.nature.com/articles/s41467-017-02300-x},\n\tdoi = {10.1038/s41467-017-02300-x},\n\tabstract = {Heterogeneous nucleation is a process that mediates the birth of many crystalline materials, but is not fully understood. Here, the authors show that the study of precritical cluster fluctuations paves new ways for the identification of polymorphism, polymorphic control and theoretical modeling.},\n\tlanguage = {en},\n\tnumber = {1},\n\turldate = {2018-10-07},\n\tjournal = {Nature Communications},\n\tauthor = {Fitzner, Martin and Sosso, Gabriele C. and Pietrucci, Fabio and Pipolo, Silvio and Michaelides, Angelos},\n\tmonth = dec,\n\tyear = {2017},\n\tpages = {2257},\n\tfile = {Full Text PDF:/Users/wolf/Zotero/storage/TVP9FPMX/Fitzner et al. - 2017 - Pre-critical fluctuations and what they disclose a.pdf:application/pdf;Snapshot:/Users/wolf/Zotero/storage/4YHYJFU3/s41467-017-02300-x.html:text/html}\n}\n\n\n\n Heterogeneous nucleation is a process that mediates the birth of many crystalline materials, but is not fully understood. Here, the authors show that the study of precritical cluster fluctuations paves new ways for the identification of polymorphism, polymorphic control and theoretical modeling.\n
\n\n\n\n
\n\n \n \n 2016\n \n \n (3)\n \n \n
\n \n \n \n
\n \n \n\n \n \n \n \n \n \n Crystal Nucleation in Liquids: Open Questions and Future Challenges in Molecular Dynamics Simulations.\n \n \n \n \n\n\n \n Sosso, G. C.; Chen, J.; Cox, S. J.; Fitzner, M.; Pedevilla, P.; Zen, A.; and Michaelides, A.\n\n\n \n\n\n\n Chemical Reviews, 116(12): 7078–7116. June 2016.\n \n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n\n@article{sosso_crystal_2016,\n\ttitle = {Crystal {Nucleation} in {Liquids}: {Open} {Questions} and {Future} {Challenges} in {Molecular} {Dynamics} {Simulations}},\n\tvolume = {116},\n\tissn = {0009-2665, 1520-6890},\n\tshorttitle = {Crystal {Nucleation} in {Liquids}},\n\turl = {http://pubs.acs.org/doi/10.1021/acs.chemrev.5b00744},\n\tdoi = {10.1021/acs.chemrev.5b00744},\n\tlanguage = {en},\n\tnumber = {12},\n\turldate = {2018-04-16},\n\tjournal = {Chemical Reviews},\n\tauthor = {Sosso, Gabriele C. and Chen, Ji and Cox, Stephen J. and Fitzner, Martin and Pedevilla, Philipp and Zen, Andrea and Michaelides, Angelos},\n\tmonth = jun,\n\tyear = {2016},\n\tpages = {7078--7116}\n}\n\n\n\n \n\n \n \n \n \n \n \n Microscopic Mechanism and Kinetics of Ice Formation at Complex Interfaces: Zooming in on Kaolinite.\n \n \n \n \n\n\n \n Sosso, G. C.; Li, T.; Donadio, D.; Tribello, G. A.; and Michaelides, A.\n\n\n \n\n\n\n The Journal of Physical Chemistry Letters, 7(13): 2350–2355. July 2016.\n \n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n\n@article{sosso_microscopic_2016,\n\ttitle = {Microscopic {Mechanism} and {Kinetics} of {Ice} {Formation} at {Complex} {Interfaces}: {Zooming} in on {Kaolinite}},\n\tvolume = {7},\n\tissn = {1948-7185},\n\tshorttitle = {Microscopic {Mechanism} and {Kinetics} of {Ice} {Formation} at {Complex} {Interfaces}},\n\turl = {http://pubs.acs.org/doi/10.1021/acs.jpclett.6b01013},\n\tdoi = {10.1021/acs.jpclett.6b01013},\n\tlanguage = {en},\n\tnumber = {13},\n\turldate = {2018-04-16},\n\tjournal = {The Journal of Physical Chemistry Letters},\n\tauthor = {Sosso, Gabriele C. and Li, Tianshu and Donadio, Davide and Tribello, Gareth A. and Michaelides, Angelos},\n\tmonth = jul,\n\tyear = {2016},\n\tpages = {2350--2355}\n}\n\n\n\n \n\n \n \n \n \n \n \n Ice formation on kaolinite: Insights from molecular dynamics simulations.\n \n \n \n \n\n\n \n Sosso, G. C.; Tribello, G. A.; Zen, A.; Pedevilla, P.; and Michaelides, A.\n\n\n \n\n\n\n The Journal of Chemical Physics, 145(21): 211927. December 2016.\n \n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n\n@article{sosso_ice_2016,\n\ttitle = {Ice formation on kaolinite: {Insights} from molecular dynamics simulations},\n\tvolume = {145},\n\tissn = {0021-9606, 1089-7690},\n\tshorttitle = {Ice formation on kaolinite},\n\turl = {http://aip.scitation.org/doi/10.1063/1.4968796},\n\tdoi = {10.1063/1.4968796},\n\tlanguage = {en},\n\tnumber = {21},\n\turldate = {2018-04-16},\n\tjournal = {The Journal of Chemical Physics},\n\tauthor = {Sosso, Gabriele C. and Tribello, Gareth A. and Zen, Andrea and Pedevilla, Philipp and Michaelides, Angelos},\n\tmonth = dec,\n\tyear = {2016},\n\tpages = {211927}\n}\n\n\n\n
\n\n\n\n\n \n \n 2015\n \n \n (1)\n \n \n
\n \n \n \n
\n \n \n\n \n \n \n \n \n \n The Many Faces of Heterogeneous Ice Nucleation: Interplay Between Surface Morphology and Hydrophobicity.\n \n \n \n \n\n\n \n Fitzner, M.; Sosso, G. C.; Cox, S. J.; and Michaelides, A.\n\n\n \n\n\n\n Journal of the American Chemical Society, 137(42): 13658–13669. October 2015.\n \n\n\n\n
\n\n\n\n \n \nPaper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n
\n\n\n\n\n\n \n\n\n\n \n \n
Paper\n \n \n\n \n \n doi\n \n \n\n \n link\n \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n \n \n \n\n\n\n\n
\n\n\n\n@article{fitzner_many_2015,\n\ttitle = {The {Many} {Faces} of {Heterogeneous} {Ice} {Nucleation}: {Interplay} {Between} {Surface} {Morphology} and {Hydrophobicity}},\n\tvolume = {137},\n\tissn = {0002-7863, 1520-5126},\n\tshorttitle = {The {Many} {Faces} of {Heterogeneous} {Ice} {Nucleation}},\n\turl = {http://pubs.acs.org/doi/10.1021/jacs.5b08748},\n\tdoi = {10.1021/jacs.5b08748},\n\tlanguage = {en},\n\tnumber = {42},\n\turldate = {2018-04-16},\n\tjournal = {Journal of the American Chemical Society},\n\tauthor = {Fitzner, Martin and Sosso, Gabriele C. and Cox, Stephen J. and Michaelides, Angelos},\n\tmonth = oct,\n\tyear = {2015},\n\tpages = {13658--13669}\n}\n\n\n