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@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},
}