Publication

Light-Switchable Peptides with a Hemithioindigo Unit: Peptide Design, Photochromism, and Optical Spectroscopy

Kitzig, S., Thilemann, M., Cordes, T. & Rueck-Braun, K., 4-May-2016, In : Chemphyschem. 17, 9, p. 1252-1263 12 p.

Research output: Contribution to journalReview articleAcademicpeer-review

  • S. Kitzig
  • M. Thilemann
  • T. Cordes
  • Karola Rueck-Braun

This Minireview focuses on the hemithioindigo photoswitch and its use for the reversible control of three-dimensional peptide structure and related biological functions. Both the general design aspects and biophysical properties of various hemithioindigo-based chromopeptides are summarized. Hemithioindigo undergoes reversible ZE photoisomerization after absorption of visible light. The unique ultrafast switching mechanism of hemithioindigo combines picosecond isomerization kinetics with strong double-bond torsion after light absorption, making it the ideal tool for instantaneous modulation of biological structure. Various inhibitors and model peptides based on hemithioindigo are described that can directly regulate biological signaling or allow the fastest events in peptide folding to be studied. Finally, a diverse range of chromopeptides with photoswitchable -hairpin structures based on azobenzenes, stilbenes, and hemithioindigo are compared to emphasize the unique properties of hemithioindigo.

Original languageEnglish
Pages (from-to)1252-1263
Number of pages12
JournalChemphyschem
Volume17
Issue number9
Publication statusPublished - 4-May-2016

    Keywords

  • chromophores, peptides, photochromism, protein folding, time-resolved spectroscopy, PICOSECOND CONFORMATIONAL TRANSITION, 2-DIMENSIONAL INFRARED-SPECTROSCOPY, BETA-HAIRPIN PEPTIDES, OMEGA-AMINO ACIDS, PDZ DOMAIN, FOLDING KINETICS, FINGER STRUCTURE, PROTEIN-BINDING, PHOTOISOMERIZATION, DYNAMICS

ID: 33045502