Photo-control of helix content in a short peptide.
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 photoregulated. The peptide contains two cysteine residues that are cross-linked by an azobenzene derivative in an intramolecular fashion. In accordance with the design, the photoisomerization of the azobenzene cross-linker from the trans to the cis form causes a large increase in the helix content of the peptide, in water.
Kumita
J R
JR
Department of Chemistry, University of Toronto, 80 Saint George Street, Toronto M5S 3H6, Canada.
Smart
O S
OS
Woolley
G A
GA
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D007536:Isomerism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature
D010455:Peptides