Catechol-functionalized sequence-defined glycomacromolecules as covalent inhibitors of bacterial adhesion

Autor:	Laura Hartmann, Lukas Fischer, Ricarda C. Steffens, Tanja J. Paul
Rok vydání:	2020
Předmět:	Catechol Polymers and Plastics biology Organic Chemistry Lectin Bioengineering Sequence (biology) Adhesion Biochemistry Combinatorial chemistry chemistry.chemical_compound chemistry Covalent bond Concanavalin A biology.protein Binding site Mannan
Zdroj:	Polymer Chemistry. 11:6091-6096
ISSN:	1759-9962 1759-9954
Popis:	Herein, we present the synthesis of catechol functionalized sequence-defined glycomacromolecules that can covalently block the binding site of lectins and bacterial adhesins. These structures produced on a solid phase support combine two important features: the multivalent presentation of carbohydrates for specificity, and catechols as anchors to go from highly reversible interactions to covalent attachment and more efficient inhibition. In our study we demonstrate this on the lectin Concanavalin A (ConA) by showing an increase in clustering for catechol ligands and on the effective inhibition of bacterial adhesion of E. coli on mannan surfaces by our catechol functionalized glycomacromolecules. Furthermore, covalent attachment is studied via MALDI-TOF measurements and SDS-PAGE analysis. Importantly, by replacing binding sugars with non-binding sugars, no inhibitory effects or covalent attachment were observed.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::53b06a6e98ec7f4e881a06e1ff89bd53 https://doi.org/10.1039/d0py00975j Zobrazit plný text záznamu