Self-assembling peptide-polymer hydrogels designed from the coiled coil region of fibrin.

TitleSelf-assembling peptide-polymer hydrogels designed from the coiled coil region of fibrin.
Publication TypeJournal Article
Year of Publication2008
AuthorsP Jing, JS Rudra, AB Herr, and JH Collier
Start Page2438
Pagination2438 - 2446
Date Published09/2008

Biomaterials constructed from self-assembling peptides, peptide derivatives, and peptide-polymer conjugates are receiving increasing attention as defined matrices for tissue engineering, controlled therapeutic release, and in vitro cell expansion, but many are constructed from peptide structures not typically found in the human extracellular matrix. Here we report a self-assembling biomaterial constructed from a designed peptide inspired by the coiled coil domain of human fibrin, the major protein constituent of blood clots and the provisional scaffold of wound healing. Targeted substitutions were made in the residues forming the interface between coiled coil strands for a 37-amino acid peptide from human fibrinogen to stabilize the coiled coil peptide bundle, while the solvent-exposed residues were left unchanged to provide a surface similar to that of the native protein. This peptide, which self-assembled into coiled coil dimers and tetramers, was then used to produce triblock peptide-PEG-peptide bioconjugates that self-assembled into viscoelastic hydrogel biomaterials.

Short TitleBiomacromolecules