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Light and heat control over secondary structure and amyloid-like fiber formation in an overcrowded-alkene-modified Trp zipper.

Claudia PoloniMarc C A StuartPieter van der MeulenWiktor SzymanskiBen L Feringa
Published in: Chemical science (2015)
The external photocontrol over peptide folding, by the incorporation of molecular photoswitches into their structure, provides a powerful tool to study biological processes. However, it is limited so far to switches that exhibit only a rather limited geometrical change upon photoisomerization and that show thermal instability of the photoisomer. Here we describe the use of an overcrowded alkene photoswitch to control a model β-hairpin peptide. This photoresponsive unit undergoes a large conformational change and has two thermally stable isomers which has major influence on the secondary structure and the aggregation of the peptide, permitting the phototriggered formation of amyloid-like fibrils.
Keyphrases
  • single molecule
  • molecular dynamics simulations
  • molecular dynamics
  • light emitting