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Maleimide–thiol coupling of a bioactive peptide to an elastin-like protein polymer

Paper ID Volume ID Publish Year Pages File Format Full-Text
1463 84 2012 9 PDF Available
Title
Maleimide–thiol coupling of a bioactive peptide to an elastin-like protein polymer
Abstract

Recombinant elastin-like protein (ELP) polymers display several favorable characteristics for tissue repair and replacement as well as drug delivery applications. However, these materials are derived from peptide sequences that do not lend themselves to cell adhesion, migration, or proliferation. This report describes the chemoselective ligation of peptide linkers bearing the bioactive RGD sequence to the surface of ELP hydrogels. Initially, cystamine is conjugated to ELP, followed by the temperature-driven formation of elastomeric ELP hydrogels. Cystamine reduction produces reactive thiols that are coupled to the RGD peptide linker via a terminal maleimide group. Investigations into the behavior of endothelial cells and mesenchymal stem cells on the RGD-modified ELP hydrogel surface reveal significantly enhanced attachment, spreading, migration and proliferation. Attached endothelial cells display a quiescent phenotype.

Keywords
Elastin-like polypeptide; Tissue engineering; Viscoelastic; Protein polymer; Biomimetic
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Maleimide–thiol coupling of a bioactive peptide to an elastin-like protein polymer
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Publisher
Database: Elsevier - ScienceDirect
Journal: Acta Biomaterialia - Volume 8, Issue 2, February 2012, Pages 627–635
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
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us