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Cytocompatibility of self-assembled β-hairpin peptide hydrogel surfaces

Paper ID Volume ID Publish Year Pages File Format Full-Text
12316 789 2005 10 PDF Available
Title
Cytocompatibility of self-assembled β-hairpin peptide hydrogel surfaces
Abstract

MAX1 is a 20 amino acid peptide that undergoes triggered self-assembly to form a rigid hydrogel. When dissolved in aqueous solutions, this peptide exists in an ensemble of random coil conformations rendering it fully soluble. The addition of an exogenous stimulus results in peptide folding into β-hairpin conformation. This folded structure undergoes rapid assembly into a highly crosslinked hydrogel network. DMEM cell culture media is one stimulus able to initiate folding and consequent self-assembly of MAX1. The cytocompatibility of this gel towards NIH 3T3 murine fibroblasts is demonstrated. Gels were shown to be non-toxic to the fibroblast cells. MAX1 hydrogels also foster the ability of the cells to attach to the hydrogel scaffold in the absence or presence of serum proteins. Additionally MAX1 hydrogels were able to support fibroblast proliferation to confluency with little effect on the rheological properties of the scaffold. MAX1 hydrogels meet the preliminary mechanical and cytocompatibiltiy requirements of a tissue engineering scaffold.

Keywords
Cell adhesion; Cell proliferation; Cell viability; Fibroblast; Hydrogel; Peptide
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Cytocompatibility of self-assembled β-hairpin peptide hydrogel surfaces
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biomaterials - Volume 26, Issue 25, September 2005, Pages 5177–5186
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
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Online Support
Any Questions? feel free to contact us