Rapidly recovering hydrogel scaffolds from self-assembling diblock copolypeptide amphiphiles

Andrew P. Nowak, Victor Breedveld, Lisa Pakstis, Bulent Ozbas, David J. Pine, Darrin Pochan and Timothy J. Deming ()
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Andrew P. Nowak: University of California
Victor Breedveld: University of California
Lisa Pakstis: University of Delaware
Bulent Ozbas: University of Delaware
David J. Pine: University of California
Darrin Pochan: University of Delaware
Timothy J. Deming: University of California

Nature, 2002, vol. 417, issue 6887, 424-428

Abstract: Abstract Protein-based hydrogels are used for many applications, ranging from food and cosmetic thickeners to support matrices for drug delivery and tissue replacement1,2,3. These materials are usually prepared using proteins extracted from natural sources, which can give rise to inconsistent properties unsuitable for medical applications4. Recent developments have utilized recombinant DNA methods to prepare artificial protein hydrogels with specific association mechanisms and responsiveness to various stimuli5,6. Here we synthesize diblock copolypeptide amphiphiles containing charged and hydrophobic segments. Dilute solutions of these copolypeptides would be expected to form micelles; instead, they form hydrogels that retain their mechanical strength up to temperatures of about 90 °C and recover rapidly after stress. The use of synthetic materials permits adjustment of copolymer chain length and composition, which we varied to study their effect on hydrogel formation and properties. We find that gelation depends not only on the amphiphilic nature of the polypeptides, but also on chain conformations—α-helix, β-strand or random coil. Indeed, shape-specific supramolecular assembly is integral to the gelation process, and provides a new class of peptide-based hydrogels with potential for applications in biotechnology.

Date: 2002
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DOI: 10.1038/417424a

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