Biomaterials, Biodegradables and Biomimetics Research Group

Papers in Scientific Journals

Molecularly Engineered Self-Assembling Membranes for Cell-Mediated Degradation

Abstract

The use of peptide engineering to develop self-assembling membranes that are responsive to cellular enzyme activities is reported. The membranes are obtained by combining hyaluronan (HA) and a rationally designed peptide amphiphile (PA) containing a proteolytic domain (GPQGIWGQ octapeptide) sensitive to matrix metalloproteinase-1 (MMP-1). Insertion of an octapeptide in a typical PA structure does not disturb its self-assembly into fibrillar nanostructures neither the ability to form membranes with HA. In vitro enzymatic degradation with hyaluronidase and MMP-1 shows that membranes containing the MMP-1 substrate exhibit enhanced enzymatic degradation, compared with control membranes (absence of MMP-1 cleavable peptide or containing a MMP-1 insensitive sequence), being completely degraded after 7 days. Cell viability and proliferation is minimally affected by the enzymatically cleavable functionality of the membrane, but the presence of MMP-1 cleavable sequence does stimulate the secretion of MMP-1 by fibroblasts and interfere with matrix deposition, particularly the deposition of collagen. By showing cell-responsiveness to biochemical signals presented on self-assembling membranes, this study highlights the ability of modulating certain cellular activities through matrix engineering. This concept can be further explored to understand the cellular remodeling process and as a strategy to develop artificial matrices with more biomimetic degradation for tissue engineering applications.

Journal
Advanced Healthcare Materials
URL
degradation;enzyme-responsive materials;hyaluronan;matrix metalloproteinase-1;peptide amphiphiles;self-assembling membranes
Keywords
Degradation, enzyme-responsive materials, Hyaluronan, matrix metalloproteinase-1, peptide amphiphiles, self-assembling membranes
Rights
Restricted Access
Peer Reviewed
Yes
Status
published
Project
EpitHope
Year of Publication
2014
DOI
10.1002/adhm.201400586
Date Published
2014-11-21
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