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

*Bijbehorende auteur voor dit werk

OnderzoeksoutputAcademicpeer review

19 Citaten (Scopus)
346 Downloads (Pure)

Samenvatting

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.

Originele taal-2English
Pagina's (van-tot)7311-7318
Aantal pagina's8
TijdschriftChemical Science
Volume6
Nummer van het tijdschrift12
DOI's
StatusPublished - 2015

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