期刊
BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY
卷 6, 期 -, 页码 801-809出版社
BEILSTEIN-INSTITUT
DOI: 10.3762/bjoc.6.90
关键词
bacterial adhesion; bivalent ligand; ELISA; FimH; glycopeptides
资金
- Christiana Albertina University
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.
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