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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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
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author Thisbe K. Lindhorst
Kathrin Bruegge
Andreas Fuchs
Oliver Sperling
author_facet Thisbe K. Lindhorst
Kathrin Bruegge
Andreas Fuchs
Oliver Sperling
author_sort Thisbe K. Lindhorst
collection DOAJ
description 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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spelling doaj.art-e6928923ffcf4c179978809ee140f9332022-12-21T22:05:00ZengBeilstein-InstitutBeilstein Journal of Organic Chemistry1860-53972010-08-016180180910.3762/bjoc.6.901860-5397-6-90A bivalent glycopeptide to target two putative carbohydrate binding sites on FimHThisbe K. Lindhorst0Kathrin Bruegge1Andreas Fuchs2Oliver Sperling3Christiana Albertina University of Kiel, Otto Diels Institute of Organic Chemistry, Otto-Hahn-Platz 4, D-24098 Kiel, Germany, Fax: +49 431 8807410Christiana Albertina University of Kiel, Otto Diels Institute of Organic Chemistry, Otto-Hahn-Platz 4, D-24098 Kiel, Germany, Fax: +49 431 8807410Christiana Albertina University of Kiel, Otto Diels Institute of Organic Chemistry, Otto-Hahn-Platz 4, D-24098 Kiel, Germany, Fax: +49 431 8807410Christiana Albertina University of Kiel, Otto Diels Institute of Organic Chemistry, Otto-Hahn-Platz 4, D-24098 Kiel, Germany, Fax: +49 431 8807410FimH 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.https://doi.org/10.3762/bjoc.6.90bacterial adhesionbivalent ligandELISAFimHglycopeptides
spellingShingle Thisbe K. Lindhorst
Kathrin Bruegge
Andreas Fuchs
Oliver Sperling
A bivalent glycopeptide to target two putative carbohydrate binding sites on FimH
Beilstein Journal of Organic Chemistry
bacterial adhesion
bivalent ligand
ELISA
FimH
glycopeptides
title A bivalent glycopeptide to target two putative carbohydrate binding sites on FimH
title_full A bivalent glycopeptide to target two putative carbohydrate binding sites on FimH
title_fullStr A bivalent glycopeptide to target two putative carbohydrate binding sites on FimH
title_full_unstemmed A bivalent glycopeptide to target two putative carbohydrate binding sites on FimH
title_short A bivalent glycopeptide to target two putative carbohydrate binding sites on FimH
title_sort bivalent glycopeptide to target two putative carbohydrate binding sites on fimh
topic bacterial adhesion
bivalent ligand
ELISA
FimH
glycopeptides
url https://doi.org/10.3762/bjoc.6.90
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