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Light and heat control over secondary structure and amyloid-like fiber formation in an overcrowded-alkene-modified
Claudia Poloni1, Marc C A Stuart1, Pieter van der Meulen1
1Centre for Systems Chemistry , Stratingh Institute for Chemistry , Faculty of Mathematics and Natural Sciences , University of Groningen , Nijenborgh 4 , 9747AG Groningen , The Netherlands . Email: b.l.feringa@rug.nl ;
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 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.
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