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The immobilization of proteins on biodegradable fibers via biotin–streptavidin bridges

Paper ID Volume ID Publish Year Pages File Format Full-Text
1750 90 2008 8 PDF Available
Title
The immobilization of proteins on biodegradable fibers via biotin–streptavidin bridges
Abstract

This paper aims at developing novel bioactive fibrous mats for protein immobilization and for protein separation/purification. For this purpose, an amphiphilic triblock copolymer, biotinylated poly(ethylene glycol)-b-poly(l-lactide)-b-poly(l-lysine) was co-electrospun together with poly(l-lactide-co-glycolide) into ultrafine fibers ∼2 μm in diameter, and a layer of blocking agent was coated on the fiber surfaces to block off possible non-specific binding of proteins. The biotin species retained their ability to specifically recognize and bind streptavidin, and the immobilized streptavidin could further combine with biotinylated antibodies, antigens and other biological moieties. Horseradish peroxidase-labeled streptavidin and fluorescein isothiocyanate-labeled goat globulin were used to detect the immobilizations of streptavidin and rabbit anti-goat IgG(H + L) via enzyme-linked immunoassay and confocal laser scanning microscope, respectively. The immobilized antigen was eluted from the fiber substrate with a glycine/HCl solution and the eluted antigen retained its bioactivity. Therefore, these biotin-carrying composite fibers have a variety of uses, including selective immobilization of functional proteins, antigen/antibody separation and purification, and vaccine preparation.

Keywords
Electrospun fibers; Protein immobilization; Immunoassay; Antibodies; Antigens
First Page Preview
The immobilization of proteins on biodegradable fibers via biotin–streptavidin bridges
Publisher
Database: Elsevier - ScienceDirect
Journal: Acta Biomaterialia - Volume 4, Issue 6, November 2008, Pages 1770–1777
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering