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Conformational recovery and preservation of protein nature from heat-induced denaturation by water-soluble phospholipid polymer conjugation

Paper ID Volume ID Publish Year Pages File Format Full-Text
9019 615 2009 9 PDF Available
Title
Conformational recovery and preservation of protein nature from heat-induced denaturation by water-soluble phospholipid polymer conjugation
Abstract

The effect of water-soluble phospholipid polymer conjugated to a protein on conformational change during heat-quenched stress was investigated in this study. Well-defined pyridine disulfide end-functional poly(2-methacryloyloxyethyl phosphorylcholine) (PMPC) was synthesized by well controlled atom transfer radical polymerization method. Synthesized PMPC was the site specifically conjugated to a protein, and the effect on conformational change during heat-quenched stress was estimated by circular dichroism and fluorescence study. As a result, a single phospholipid polymer chain conjugated to a protein give a great effect on conformational preservation in both secondary and tertiary structures even after the heat-quenced process. Moreover, even the conformational recovery which gave the completely reversible conformational preservation was observed in circular dichroism study. The resulting protein activity was also confirmed, and no significant decline was induced by heat-quenched stress.

Keywords
Phospholipid polymer; Bioconjugation; Conformation change; Protein; Enzyme
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Conformational recovery and preservation of protein nature from heat-induced denaturation by water-soluble phospholipid polymer conjugation
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biomaterials - Volume 30, Issue 28, October 2009, Pages 4859–4867
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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