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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Format: | Article |
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Beilstein-Institut
2010-08-01
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Series: | Beilstein Journal of Organic Chemistry |
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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. |
first_indexed | 2024-12-17T03:41:38Z |
format | Article |
id | doaj.art-e6928923ffcf4c179978809ee140f933 |
institution | Directory Open Access Journal |
issn | 1860-5397 |
language | English |
last_indexed | 2024-12-17T03:41:38Z |
publishDate | 2010-08-01 |
publisher | Beilstein-Institut |
record_format | Article |
series | Beilstein Journal of Organic Chemistry |
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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