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Thermally Reversible Hydrogels via Intramolecular Folding and Consequent Self-Assembly of a de Novo Designed Peptide
Abstract
A small de novo designed peptide (MAX3) is described that exhibits complete thermoreversible self-assembly into a hydrogel network. Importantly, a prerequisite to hydrogelation is that the peptide must first fold into a conformation conducive to self-assembly. At ambient temperature, MAX3 is unfolded, resulting in a low viscosity aqueous solution. On increasing the temperature, the peptide undergoes a unimolecular folding event, affording an amphiphilic beta-hairpin that consequently self-assembles into a hydrogel network. Increasing the temperature serves to dehydrate the nonpolar residues of the unfolded peptide and trigger folding via hydrophobic collapse. Cooling the resultant hydrogel results in beta-hairpin unfolding and consequent complete dissolution of the hydrogel. The temperature at which folding and consequent self-assembly into a rigid hydrogel occur can be tuned by altering the hydrophobicity of the peptides.
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Citations
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Metadata
- Authors
- Pochan, D. J., Schneider, J. P., Kretsinger, J., Ozbas, B., Rajagopal, K., & Haines, L.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2003-09-06
- Volume
- 125
- Issue
- 39
- Pages
- 11802-11803
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W1985367101
- Cited by
- 463
- References
- 0
- FWCI
- 7.14
- Type
- journal article
- Language
- en
- Open access
- closed
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