A minimalistic cyclic ice-binding peptide from phage display. Stevens, C. A., Bachtiger, F., Kong, X., Abriata, L. A., Sosso, G. C., Gibson, M. I., & Klok, H. Nature Communications, 12(1):2675, May, 2021. Bandiera_abtest: a Cc_license_type: cc_by Cg_type: Nature Research Journals Number: 1 Primary_atype: Research Publisher: Nature Publishing Group Subject_term: Biopolymers;Peptides Subject_term_id: biopolymers;peptides![A minimalistic cyclic ice-binding peptide from phage display [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Developing molecules that emulate the properties of naturally occurring ice-binding proteins (IBPs) is a daunting challenge. Rather than relying on the (limited) existing structure–property relationships that have been established for IBPs, here we report the use of phage display for the identification of short peptide mimics of IBPs. To this end, an ice-affinity selection protocol is developed, which enables the selection of a cyclic ice-binding peptide containing just 14 amino acids. Mutational analysis identifies three residues, Asp8, Thr10 and Thr14, which are found to be essential for ice binding. Molecular dynamics simulations reveal that the side chain of Thr10 hydrophobically binds to ice revealing a potential mechanism. To demonstrate the biotechnological potential of this peptide, it is expressed as a fusion (‘Ice-Tag’) with mCherry and used to purify proteins directly from cell lysate.
@article{stevens_minimalistic_2021,
title = {A minimalistic cyclic ice-binding peptide from phage display},
volume = {12},
copyright = {2021 The Author(s)},
issn = {2041-1723},
url = {https://www.nature.com/articles/s41467-021-22883-w},
doi = {10.1038/s41467-021-22883-w},
abstract = {Developing molecules that emulate the properties of naturally occurring ice-binding proteins (IBPs) is a daunting challenge. Rather than relying on the (limited) existing structure–property relationships that have been established for IBPs, here we report the use of phage display for the identification of short peptide mimics of IBPs. To this end, an ice-affinity selection protocol is developed, which enables the selection of a cyclic ice-binding peptide containing just 14 amino acids. Mutational analysis identifies three residues, Asp8, Thr10 and Thr14, which are found to be essential for ice binding. Molecular dynamics simulations reveal that the side chain of Thr10 hydrophobically binds to ice revealing a potential mechanism. To demonstrate the biotechnological potential of this peptide, it is expressed as a fusion (‘Ice-Tag’) with mCherry and used to purify proteins directly from cell lysate.},
language = {en},
number = {1},
urldate = {2021-06-22},
journal = {Nature Communications},
author = {Stevens, Corey A. and Bachtiger, Fabienne and Kong, Xu-Dong and Abriata, Luciano A. and Sosso, Gabriele C. and Gibson, Matthew I. and Klok, Harm-Anton},
month = may,
year = {2021},
note = {Bandiera\_abtest: a
Cc\_license\_type: cc\_by
Cg\_type: Nature Research Journals
Number: 1
Primary\_atype: Research
Publisher: Nature Publishing Group
Subject\_term: Biopolymers;Peptides
Subject\_term\_id: biopolymers;peptides},
pages = {2675},
}
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