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PubMed · 11927265

Using an azobenzene cross-linker to either increase or decrease peptide helix content upon trans-to-cis photoisomerization.

Daniel G Flint·Janet R Kumita·Oliver S Smart·G Andrew Woolley
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Abstract

Reversible photocontrol of peptide and protein conformation could prove to be a powerful tool for probing function in diverse biological systems. Here, we report reversible photoswitching of the helix content in short peptides containing an azobenzene cross-linker between cysteine residues at positions i, i + 4, or i, i + 11 in the sequence. Trans-to-cis photoisomerization significantly increases the helix content in the i, i + 4 case and significantly decreases the helix content in the i, i + 11 case. These cross-linker designs significantly expand the possibilities for photocontrol of peptide and protein structure.

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Azo CompoundsCross-Linking ReagentsModels, MolecularPeptidesProtein Structure, SecondaryStereoisomerismJournal ArticleResearch Support, Non-U.S. Gov't

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Daniel G Flint, Janet R Kumita, Oliver S Smart, G Andrew Woolley. 2002. Using an azobenzene cross-linker to either increase or decrease peptide helix content upon trans-to-cis photoisomerization.. https://doi.org/10.1016/s1074-5521(02)00109-6

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