Architecture Effects on the Binding of Cholera Toxin by Helical Glycopolypeptides.

ABSTRACT: A variety of binding events in biological systems are mediated by multivalent interactions between oligosaccharides and saccharide receptors present on pathogens and cell surfaces. In particular, given the important role of multivalent interaction between proteins and carbohydrates in the initial step of pathogen recognition, many glycosylated molecules and polymers have been synthesized in order to mimic the carbohydrate ligands and to inhibit the binding of the pathogen to its target. In this work, we extend our evaluation of the impact of the architecture of well-defined glycopolypeptides on the inhibition of binding of the cholera toxin B pentamer (CT B(5)) subunit. Here we report the production of two families of α-helical glycopolypeptides which were synthesized via a combination of

SUBMITTER: Liu S 

PROVIDER: S-EPMC2639716 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature