The alpha-helix is a key structural element in a wide range of peptides and
proteins. We report here the design, synthesis, and characterization of a
modified peptide in which the helix content can be reversibly photoregulate
d, The peptide contains two cysteine residues that are cross-linked by an a
zobenzene derivative in an intramolecular fashion. In accordance with the d
esign, the photoisomerization of the azobenzene cross-linker from the trans
to the cis form causes a large increase in the helix content of the peptid
e, in water.