Light and heat control over secondary structure and amyloid-like fiber formation in an overcrowded-alkene-modified Trp zipper
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Authors: | Claudia Poloni Marc C A Stuart Pieter van der Meulen Wiktor Szymanski Ben L Feringa |
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Institution: | a Centre for Systems Chemistry , Stratingh Institute for Chemistry , Faculty of Mathematics and Natural Sciences , University of Groningen , Nijenborgh 4 , 9747AG Groningen , The Netherlands . Email: ; Email: ; Fax: +31-50-3634279 ; b Department of Radiology , University of Groningen , University Medical Center Groningen , Hanzeplein 1 , 9713 GZ , Groningen , The Netherlands |
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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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