Reversible photocontrol of peptide conformation with a rhodopsin-like photoswitch

  1. Blanco-Lomas, M. 1
  2. Samanta, S. 2
  3. Campos, P.J. 1
  4. Woolley, G.A. 2
  5. Sampedro, D. 1
  1. 1 Universidad de La Rioja
    info

    Universidad de La Rioja

    Logroño, España

    ROR https://ror.org/0553yr311

  2. 2 University of Toronto
    info

    University of Toronto

    Toronto, Canadá

    ROR https://ror.org/03dbr7087

Revista:
Journal of the American Chemical Society

ISSN: 0002-7863

Año de publicación: 2012

Volumen: 134

Número: 16

Páginas: 6960-6963

Tipo: Artículo

DOI: 10.1021/JA301868P PMID: 22482865 SCOPUS: 2-s2.0-84860321920 WoS: WOS:000303139800019 GOOGLE SCHOLAR

Otras publicaciones en: Journal of the American Chemical Society

Resumen

Reversible photocontrol of biomolecules requires chromophores that can efficiently undergo large conformational changes upon exposure to wavelengths of light that are compatible with living systems. We designed a benzylidene-pyrroline chromophore that mimics the Schiff base of rhodopsin and can be used to introduce light-switchable intramolecular cross-links in peptides and proteins. This new class of photoswitch undergoes an ∼10 Å change in end-to-end distance upon isomerization and can be used to control the conformation of a target peptide efficiently and reversibly using, alternately, violet (400 nm) and blue (446 nm) light. © 2012 American Chemical Society.