31 research outputs found
Multivalent glycoconjugates as anti-pathogenic agents
Multivalency plays a major role in biological processes and particularly in the relationship between pathogenic microorganisms and their host
that involves protein–glycan recognition. These interactions occur during the first steps of infection, for specific recognition between host and
bacteria, but also at different stages of the immune response. The search for high-affinity ligands for studying such interactions involves the
combination of carbohydrate head groups with different scaffolds and linkers generating multivalent glycocompounds with controlled spatial
and topology parameters. By interfering with pathogen adhesion, such glycocompounds including glycopolymers, glycoclusters,
glycodendrimers and glyconanoparticles have the potential to improve or replace antibiotic treatments that are now subverted by resistance.
Multivalent glycoconjugates have also been used for stimulating the innate and adaptive immune systems, for example with carbohydrate-based
vaccines. Bacteria present on their surfaces natural multivalent glycoconjugates such as lipopolysaccharides and S-layers that can also be
exploited or targeted in anti-infectious strategie
Reactivity Tournament of Isothiocyanato-Functionalized Saccharides with 1,6-Diamino-3,6-oxaoctane
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 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