Recombinant Protein-co-PEG Networks as Cell-Adhesive and Proteolytically Degradable Hydrogel Matrixes. Part 1: Development and Physicochemical Characteristics

Rizzi, Simone C. & Hubbell, Jeffrey A. (2005) Recombinant Protein-co-PEG Networks as Cell-Adhesive and Proteolytically Degradable Hydrogel Matrixes. Part 1: Development and Physicochemical Characteristics. Biomacromolecules, 6(3), pp. 1226-1238.

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Toward the development of synthetic bioactive materials to support tissue repair, we present here the design, production, and characterization of genetically engineered protein polymers carrying specific key features of the natural extracellular matrix, as well as cross-linking with functionalized poly(ethylene glycol) (PEG) to form hybrid hydrogel networks. The repeating units of target recombinant protein polymers contain a cell-binding site for ligation of cell-surface integrin receptors and substrates for plasmin and matrix metalloproteinases (MMPs), proteases implicated in wound healing and tissue regeneration. Hydrogels were formed under physiological conditions via Michael-type conjugate addition of vinyl sulfone groups of end-functionalized PEG with thiols of cysteine residues, representing designed chemical cross-linking sites within recombinant proteins. Cross-linking kinetics was shown to increase with the pH of precursor solutions. The elastic moduli (G') and swelling ratios (Qm) of the resulting hydrogels could be varied as a function of the stoichiometry of the reacting groups and precursor concentration. Optima of G' and Qm, maximum and minimum, respectively, were obtained at stoichiometry ratios r slightly in excess of 1 (r = cysteine/vinyl sulfone). The pool of technologies utilized here represents a promising approach for the development of artificial matrixes tailored for specific medical applications.

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ID Code: 10382
Item Type: Journal Article
Refereed: Yes
Additional Information: This article is freely available from the American Chemical Society website 12 months after the publication date. See links to publisher website in this record.
DOI: 10.1021/bm049614c
ISSN: 1525-7797
Divisions: Past > QUT Faculties & Divisions > Faculty of Science and Technology
Copyright Owner: Copyright 2003 American Chemical Society
Copyright Statement: The contents of this journal can be freely accessed online via the ACS web page 12 months after publication. See link to ACS website.
Deposited On: 25 Oct 2007 00:00
Last Modified: 29 Feb 2012 13:21

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