Modulation of the peptide backbone conformation by the selenoxo photoswitch. Academic Article uri icon

Overview

abstract

  • Photocontrol of the backbone conformation is a useful step forward in regulating the bioactivities of peptides and proteins by means of external signals. In the present work, the selenium analogue of a peptide bond was introduced into tetrapeptides to obtain surprisingly stable selenoxo peptides. Selenoxo peptide bonds allow for a marked increase of cis content in the photostationary state of peptide chains when irradiated with UV light near 290 nm. Slow thermal re-equilibration with rate constants between 9.9 x 10(-4) and 1.3 x 10(-5) s(-1) shows that the transient nonequilibrium conformations exist long enough to monitor the isomer specificity of biochemical reactions.

publication date

  • June 9, 2010

Research

keywords

  • Peptides
  • Selenium Compounds

Identity

Scopus Document Identifier

  • 77953112894

Digital Object Identifier (DOI)

  • 10.1021/ja1019386

PubMed ID

  • 20481495

Additional Document Info

volume

  • 132

issue

  • 22