Gels by Reduction

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Science  07 May 2010:
Vol. 328, Issue 5979, pp. 669
DOI: 10.1126/science.328.5979.669-c

Short linear peptides have a propensity to assemble in solution into β-sheet structures that can form gels. Bowerman and Nilsson describe a strategy for triggering gelation through reduction. They took an amphipathic peptide sequence, (Phe-Lys-Phe-Glu)2, and flanked it with cysteine residues and a glycine at the C terminus. The peptide was released into a water-acetonitrile solution and cyclized at the cysteine sites through disulfide bond formation. When diluted in aqueous solution, this cyclic peptide had no tendency to form secondary structures. However, when exposed to a reductant, such as dithiothreitol or tris(2-carboxyethyl)phosphine, to break the S-S bond, the linear form could produce hydrogels at 10 mM concentrations. Such triggers might be exploited within cells or tissues where changes in reducing conditions can occur.

J. Am. Chem. Soc. 132, 10.1021/ja1025535 (2010).

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