Structural Considerations for Building Synthetic Glycoconjugates as Inhibitors for Pseudomonas aeruginosa Lectins. Wojtczak, K. & Byrne, J. P. ChemMedChem, 17(12):e202200081, 2022. _eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1002/cmdc.202200081![Structural Considerations for Building Synthetic Glycoconjugates as Inhibitors for Pseudomonas aeruginosa Lectins [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Pseudomonas aeruginosa is a pathogenic bacterium, responsible for a large portion of nosocomial infections globally and designated as critical priority by the World Health Organisation. Its characteristic carbohydrate-binding proteins LecA and LecB, which play a role in biofilm-formation and lung-infection, can be targeted by glycoconjugates. Here we review the wide range of inhibitors for these proteins (136 references), highlighting structural features and which impact binding affinity and/or therapeutic effects, including carbohydrate selection; linker length and rigidity; and scaffold topology, particularly for multivalent candidates. We also discuss emerging therapeutic strategies, which build on targeting of LecA and LecB, such as anti-biofilm activity, anti-adhesion and drug-delivery, with promising prospects for medicinal chemistry.
@article{wojtczak_structural_2022,
title = {Structural {Considerations} for {Building} {Synthetic} {Glycoconjugates} as {Inhibitors} for {Pseudomonas} aeruginosa {Lectins}},
volume = {17},
copyright = {All rights reserved},
issn = {1860-7187},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/cmdc.202200081},
doi = {10.1002/cmdc.202200081},
abstract = {Pseudomonas aeruginosa is a pathogenic bacterium, responsible for a large portion of nosocomial infections globally and designated as critical priority by the World Health Organisation. Its characteristic carbohydrate-binding proteins LecA and LecB, which play a role in biofilm-formation and lung-infection, can be targeted by glycoconjugates. Here we review the wide range of inhibitors for these proteins (136 references), highlighting structural features and which impact binding affinity and/or therapeutic effects, including carbohydrate selection; linker length and rigidity; and scaffold topology, particularly for multivalent candidates. We also discuss emerging therapeutic strategies, which build on targeting of LecA and LecB, such as anti-biofilm activity, anti-adhesion and drug-delivery, with promising prospects for medicinal chemistry.},
language = {en},
number = {12},
urldate = {2022-09-07},
journal = {ChemMedChem},
author = {Wojtczak, Karolina and Byrne, Joseph P.},
year = {2022},
note = {\_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1002/cmdc.202200081},
pages = {e202200081},
}
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