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Macromolecules. 2008 Feb 12;41(3):764-772.

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

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1
University of Delaware.

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 protein engineering and chemical methods. The presentation of pendant saccharides on the polypeptide backbones, as well as their valencies, can be well controlled via these methods. Control of the backbone conformation, introduced in this report, is also possible via these strategies. The polypeptides and glycopolypeptides were characterized via SDS-PAGE analysis, (1)H NMR, and MALDI-TOF mass spectrometry. Their conformation and hydrodynamic volume were characterized by circular dichroic (CD) spectroscopy and gel permeation chromatography (GPC), respectively. The binding of CT B(5) by these glycopolypeptides was evaluated via direct enzyme-linked immunosorbent assay (DELA). The effects of spacing and conformation were elucidated by comparison of the binding exhibited by helical glycopolypeptides with that of random-coil glycopolypeptides.

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