Unknown

Dataset Information

0

Structural Considerations for Building Synthetic Glycoconjugates as Inhibitors for Pseudomonas aeruginosa Lectins.


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.

SUBMITTER: Wojtczak K 

PROVIDER: S-EPMC9321714 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structural Considerations for Building Synthetic Glycoconjugates as Inhibitors for Pseudomonas aeruginosa Lectins.

Wojtczak Karolina K   Byrne Joseph P JP  

ChemMedChem 20220503 12


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  ...[more]

Similar Datasets

| S-EPMC11753388 | biostudies-literature
| S-EPMC7062425 | biostudies-literature
| S-EPMC4434466 | biostudies-literature
| S-EPMC6783499 | biostudies-literature
| S-EPMC6333909 | biostudies-literature
| S-EPMC3723537 | biostudies-literature
| S-EPMC7586336 | biostudies-literature
| S-EPMC1137519 | biostudies-other
| S-EPMC3008242 | biostudies-literature
| S-EPMC8655052 | biostudies-literature