RESUMEN
We redox-regulated alpha-helicity of short peptides intramolecularly cross-linked with a ferrocenyl linker between amino acid side chains. The helical content of the cross-linked peptide was estimated to be 56% in the neutral state of the ferrocene core at 25 degrees C. The addition of an oxidant to the solution of the cross-linked peptide enhanced the helicity up to 75%. The increased helical content returned to the same level as that in the previous ferrocene state by further addition of a reductant.
Asunto(s)
Compuestos Ferrosos/química , Péptidos/química , Secuencia de Aminoácidos , Oxidación-Reducción , Conformación ProteicaRESUMEN
[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.