The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Reversible Hydrogels from Self-Assembling Artificial Proteins
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.
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Citations
Cites
Predicting coiled coils from protein sequences.
Lupas, A., Van Dyke, M., & Stock, J. (1991) · Science · doi:10.1126/science.252.5009.1162 · Cited by 3,953
The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins
Landschulz, W. H., Johnson, P. F., & McKnight, S. L. (1988) · Science · doi:10.1126/science.3289117 · Cited by 3,443
Mechanism of specificity in the Fos-Jun oncoprotein heterodimer
O'Shea, E. K., Rutkowski, R., & Kim, P. S. (1992) · Cell · doi:10.1016/0092-8674(92)90145-3 · Cited by 422
A Buried Polar Interaction Imparts Structural Uniqueness in a Designed Heterodimeric Coiled Coil
Lumb, K. J., & Kim, P. S. (1995) · Biochemistry · doi:10.1021/bi00027a013 · Cited by 266
Cited by
Lutolf, M. P., & Hubbell, J. A. (2005) · Nature Biotechnology · doi:10.1038/nbt1055 · Cited by 4,551
Hydrogels in Biology and Medicine: From Molecular Principles to Bionanotechnology
Peppas, N. A., Hilt, J. Z., Khademhosseini, A., & Langer, R. (2006) · Advanced Materials · doi:10.1002/adma.200501612 · Cited by 4,109
Biomaterials: Where We Have Been and Where We Are Going
Ratner, B. D., & Bryant, S. J. (2004) · Annual Review of Biomedical Engineering · doi:10.1146/annurev.bioeng.6.040803.140027 · Cited by 1,507
Hydrogels in a historical perspective: From simple networks to smart materials
Buwalda, S. J., Boere, K. W. M., Dijkstra, P. J., Feijen, J., Vermonden, T., & Hennink, W. E. (2014) · Journal of Controlled Release · doi:10.1016/j.jconrel.2014.03.052 · Cited by 994
The Design of Coiled-Coil Structures and Assemblies
Woolfson, D. N. (2005) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(05)70004-8 · Cited by 585
Metadata
- Authors
- Petka, W. A., Harden, J. L., McGrath, K. P., Wirtz, D., & Tirrell, D. A.
- Venue
- Science
- Published
- 1998-07-17
- Volume
- 281
- Issue
- 5375
- Pages
- 389-392
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2087208805
- Cited by
- 1,076
- References
- 4
- FWCI
- 23.72
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
