Does targeting Arg98 of FimH lead to high affinity antagonists?
Antagonist
Antiadhesive agent
Biofilm
FimH
Urinary tract infection
Journal
European journal of medicinal chemistry
ISSN: 1768-3254
Titre abrégé: Eur J Med Chem
Pays: France
ID NLM: 0420510
Informations de publication
Date de publication:
05 Feb 2021
05 Feb 2021
Historique:
received:
28
09
2020
revised:
20
11
2020
accepted:
06
12
2020
pubmed:
20
12
2020
medline:
1
5
2021
entrez:
19
12
2020
Statut:
ppublish
Résumé
Bacterial resistance has become an important challenge in the treatment of urinary tract infections. The underlying resistance mechanisms can most likely be circumvented with an antiadhesive approach, antagonizing the lectin FimH located at the tip of fimbriae of uropathogenic E. coli. Here we report on a novel series of FimH antagonists based on the 1-(α-d-mannopyranosyl)-4-phenyl-1,2,3-triazole scaffold, designed to incorporate carboxylic acid or ester functions to interact with FimH Arg98. The most potent representative of the series, ester 11e, displayed a K
Identifiants
pubmed: 33340913
pii: S0223-5234(20)31065-5
doi: 10.1016/j.ejmech.2020.113093
pii:
doi:
Substances chimiques
Adhesins, Escherichia coli
0
fimH protein, E coli
0
Fimbriae Proteins
147680-16-8
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
113093Informations de copyright
Copyright © 2020 Elsevier Masson SAS. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.