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

Claudia Poloni, Marc C. A. Stuart, Pieter van der Meulen, Wiktor Szymanski*, Ben L. Feringa

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

19 Citations (Scopus)
349 Downloads (Pure)

Abstract

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 beta-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.

Original languageEnglish
Pages (from-to)7311-7318
Number of pages8
JournalChemical Science
Volume6
Issue number12
DOIs
Publication statusPublished - 2015

Keywords

  • BETA-HAIRPIN PEPTIDE
  • NILE RED
  • ALZHEIMERS-DISEASE
  • TURN NUCLEATION
  • AGGREGATION
  • DYNAMICS
  • ISOMERIZATION
  • ASSEMBLIES
  • MORPHOLOGY
  • HYDROGELS

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