Using an azobenzene cross-linker to either increase or decrease peptide helix content upon trans-to-cis photoisomerization.
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.
Flint
Daniel G
DG
School of Biosciences, University of Birmingham, Edgbaston, United Kingdom.
Kumita
Janet R
JR
Smart
Oliver S
OS
Woolley
G Andrew
GA
D001391:Azo Compounds / Q000737:chemistry*; D003432:Cross-Linking Reagents / Q000737:chemistry*; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013237:Stereoisomerism
D001391:Azo Compounds; D003432:Cross-Linking Reagents; D010455:Peptides; C009850:azobenzene