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

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.

Statistics

050100'04'05'06'07'08'09'10'11'12'13'14'15'16'17
Citations per Year

157 Citations

Semantic Scholar estimates that this publication has 157 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Flint2002UsingAA, title={Using an azobenzene cross-linker to either increase or decrease peptide helix content upon trans-to-cis photoisomerization.}, author={Daniel G Flint and Janet R Kumita and Oliver S. Smart and G. Andrew Woolley}, journal={Chemistry & biology}, year={2002}, volume={9 3}, pages={391-7} }