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Artificial Protein Hydrogel Materials

Published online by Cambridge University Press:  15 February 2011

W. A. Petka ,
J. L. Harden ,
J. K. Sakata  and
D. A. Tirrell
W. A. Petka
Affiliation:
Department of Polymer Science and Engineering University of Massachusetts, Amherst, MA 01003
J. L. Harden
Affiliation:
Department of Chemical Engineering Johns Hopkins University, Baltimore, MD 21218
J. K. Sakata
Affiliation:
Department of Polymer Science and Engineering University of Massachusetts, Amherst, MA 01003 Division of Chemistry and Chemical Engineering California Institute of Technology, Pasadena, CA 91125
D. A. Tirrell
Affiliation:
Division of Chemistry and Chemical Engineering California Institute of Technology, Pasadena, CA 91125
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Abstract

Recombinant DNA methods were used to create a new class of artificial proteins that undergo reversible gelation in response to changes in pH or temperature. These proteins consist of terminal a-helical “leucine zipper” domains flanking a central, water-soluble polvelectrolyte segment. The formation of coiled-coil aggregates of the terminal domains in near-neutral pH solution triggers formation of a polymer hydrogel, with the central polyelectrolyte segment retaining solvent and preventing precipitation of the chains. Dissociation of the coiled-coil aggregates through elevation of pH or temperature causes dissolution of the gel and a return to the viscous behavior characteristic of a polymer solution. The pH and temperature range of the hydrogel state and its viscoelastic properties may be systematically varied through precise changes of the length, composition and charge density of the terminal and central blocks. Such control is of value in designing hydrogels with predetermined physical properties and makes these biosynthetic triblock copolymer systems attractive candidates for use in molecular and cellular encapsulation and in controlled reagent delivery.

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