Reversible photoregulation of helical structures in short peptides under indoor lighting/dark conditions.
[reaction: see text] A photochromic cross-linking agent with a spiropyran skeleton was developed for the reversible photoregulation of helical structures in short peptides. The helical contents of the cross-linked peptides could be regulated by ambient light and dark conditions at room temperature. This switching of the helical contents could be repeated several times without substantial loss of any activity.
Fujimoto
Kazuhisa
K
Faculty of Pharmaceutical Sciences, University of Toyama, Japan. fujimoto@ms.toyama-mpu.ac.jp
Amano
Miwo
M
Horibe
Yohei
Y
Inouye
Masahiko
M
D003432:Cross-Linking Reagents / Q000138:chemical synthesis* / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D010777:Photochemistry; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
D003432:Cross-Linking Reagents; D010455:Peptides