Kinetic studies of protein-carbohydrate interactions at the bilayer interface of catanionic vesicles

Loading...
Thumbnail Image
Authors
Islam, Mohammad R.
Advisors
English, Douglas S.
Issue Date
2010-04-23
Type
Conference paper
Keywords
Research Projects
Organizational Units
Journal Issue
Citation
Islam, Mohammad R. (2010). Kinetic studies of protein-carbohydrate interactions at the bilayer interface of catanionic vesicles. -- In Proceedings: 6th Annual Symposium: Graduate Research and Scholarly Projects. Wichita, KS: Wichita State University, p. 125-126
Abstract

In this paper, we describe our work on surface functionalization and modification of catanionic vesicles with an aim toward increasing their range of applications. Conventional vesicles are formed from double-tailed phospholipids and have important roles in biology. Unlike conventional phospholipids vesicles, aqueous mixtures of cationic and anionic single-tailed surfactants can spontaneously form unilamellar vesicles without sonication or extrusion. These vesicles dubbed “catanionic vesicles” in the literature are extremely stable with respect to salt and pH and are composed of inexpensive components. They are promising candidates for a variety of biotechnological applications including drug delivery and vaccine development. Our studies report that the ability to control the distribution of glycoconjugates in the vesicle bilayer surface provides a method to study protein-carbohydrate multivalent binding kinetics in a biomimetic environment. In this work, the exterior of catanionic vesicles was controllably functionalized by insertion of the hydrocarbon chain of the glycoconjugate n-dodecyl- β -D-glucopyranoside (C₁₂-glucose) at varying concentrations. We demonstrate how this platform consisting of a carbohydrate functionalized bilayer can be use to evaluate binding inhibitors for the lectin ConA.

Table of Contents
Description
Paper presented to the 6th Annual Symposium on Graduate Research and Scholarly Projects (GRASP) held at the Hughes Metropolitan Complex, Wichita State University, April 23, 2010.
Research completed at the Department of Chemistry, College of Liberal Arts and Sciences
Publisher
Wichita State University. Graduate School
Journal
Book Title
Series
GRASP
v.6
PubMed ID
DOI
ISSN
EISSN