Ontology highlight
ABSTRACT:
SUBMITTER: Roos G
PROVIDER: S-EPMC4027451 | biostudies-literature | 2013 Nov
REPOSITORIES: biostudies-literature
Roos Goedele G Wellens Adinda A Touaibia Mohamed M Yamakawa Nao N Geerlings Paul P Roy René R Wyns Lode L Bouckaert Julie J
ACS medicinal chemistry letters 20130913 11
Antagonists of the FimH adhesin, a protein almost universally present at the extremity of type-1 fimbriae expressed by Escherichia coli, have been abundantly in the spotlight as alternative treatments of urinary tract infections. The antagonists function as bacterial antiadhesives through highly specific α-d-mannose binding in a charged and polar pocket at the tip of the FimH lectin domain and by the stacking of alkyl or aromatic moieties substituted on the mannose with two tyrosine residues (Ty ...[more]