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

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dc.contributor.advisor	English, Douglas S.
dc.contributor.author	Islam, Mohammad R.
dc.date.accessioned	2010-09-23T15:06:35Z
dc.date.available	2010-09-23T15:06:35Z
dc.date.issued	2010-04-23
dc.identifier.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	en
dc.identifier.uri	http://hdl.handle.net/10057/3203
dc.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.	en
dc.description	Research completed at the Department of Chemistry, College of Liberal Arts and Sciences	en
dc.description.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.	en
dc.format.extent	187416 bytes
dc.format.extent	1843 bytes
dc.format.mimetype	application/pdf
dc.format.mimetype	text/plain
dc.language.iso	en_US	en
dc.publisher	Wichita State University. Graduate School	en
dc.relation.ispartofseries	GRASP	en
dc.relation.ispartofseries	v.6	en
dc.title	Kinetic studies of protein-carbohydrate interactions at the bilayer interface of catanionic vesicles	en
dc.type	Conference paper	en