Reversible hydrogels from self-assembling artificial proteins

Wendy A. Petka, James L. Harden, Kevin P. McGrath, Denis Wirtz, David A. Tirrell

Research output: Contribution to journalArticle

Abstract

Recombinant DNA methods were used to create artificial proteins that undergo reversible gelation in response to changes in pH or temperature. The proteins consist of terminal leucine zipper domains flanking a central, flexible, water-soluble polyelectrolyte segment. Formation of coiled-coil aggregates of the terminal domains in near-neutral aqueous solutions triggers formation of a three-dimensional polymer network, with the polyelectrolyte segment retaining solvent and preventing precipitation of the chain. Dissociation of the coiled-coil aggregates through elevation of pH or temperature causes dissolution of the gel and a return to the viscous behavior that is characteristic of polymer solutions. The mild conditions under which gel formation can be controlled (near-neutral pH and near- ambient temperature) suggest that these materials have potential in bioengineering applications requiring encapsulation or controlled release of molecular and cellular species.

Original languageEnglish (US)
Pages (from-to)389-392
Number of pages4
JournalScience
Volume281
Issue number5375
DOIs
StatePublished - Jul 17 1998

ASJC Scopus subject areas

  • General

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    Petka, W. A., Harden, J. L., McGrath, K. P., Wirtz, D., & Tirrell, D. A. (1998). Reversible hydrogels from self-assembling artificial proteins. Science, 281(5375), 389-392. https://doi.org/10.1126/science.281.5375.389