The inverse temperature transition exhibited by elastin-like polypeptides has been shown to provide a basis for an intriguing array of energy transduction processes. For example, the elastin poly(pentapeptide) 1 can be fabricated into cross-linked gels that remain swollen in water at temperatures below 25 °C but then deswell, or contract, upon a rise in temperature. Modification of sequence 1 has produced a series of related polypeptides that undergo phase mixing or swelling transitions in response to changes in pH, ionic strength, pressure, and oxidation/reduction or upon enzymatic phosphorylation. We report herein the photomodulation of the inverse temperature transition of the modified elastin polypeptide 2b. This development provides a route to protein-based polymeric materials and gels capable of photomechanical transduction.
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Strzegowski et al. (1994) studied this question.