Reversible Hydrogels from Self-Assembling Artificial Proteins
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 aggregat...
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Published in | Science (American Association for the Advancement of Science) Vol. 281; no. 5375; pp. 389 - 392 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Society for the Advancement of Science
17.07.1998
American Association for the Advancement of Science The American Association for the Advancement of Science |
Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0036-8075 1095-9203 |
DOI: | 10.1126/science.281.5375.389 |