A bivalent glycopeptide to target two putative carbohydrate binding sites on FimH

FimH is a mannose-specific bacterial lectin found on type 1 fimbriae with a monovalent carbohydrate recognition domain (CRD) that is known from X-ray studies. However, binding studies with multivalent ligands have suggested an additional carbohydrate-binding site on this protein. In order to prove t...

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Bibliographic Details
Main Authors: Thisbe K. Lindhorst, Kathrin Bruegge, Andreas Fuchs, Oliver Sperling
Format: Article
Language:English
Published: Beilstein-Institut 2010-08-01
Series:Beilstein Journal of Organic Chemistry
Subjects:
Online Access:https://doi.org/10.3762/bjoc.6.90
Description
Summary:FimH is a mannose-specific bacterial lectin found on type 1 fimbriae with a monovalent carbohydrate recognition domain (CRD) that is known from X-ray studies. However, binding studies with multivalent ligands have suggested an additional carbohydrate-binding site on this protein. In order to prove this hypothesis, a bivalent glycopeptide ligand with the capacity to bridge two putative carbohydrate binding sites on FimH was designed and synthesized. Anti-adhesion assays with the new bivalent ligand and type 1-fimbriated bacteria have revealed, that verification of the number of carbohydrate binding sites on FimH with a tailor-made bivalent glycopeptide requires further investigation to be conclusive.
ISSN:1860-5397