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Issue 12, 2015
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Light and heat control over secondary structure and amyloid-like fiber formation in an overcrowded-alkene-modified Trp zipper

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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.

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

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Publication details

The article was received on 27 Jul 2015, accepted on 18 Sep 2015 and first published on 23 Sep 2015


Article type: Edge Article
DOI: 10.1039/C5SC02735G
Citation: Chem. Sci., 2015,6, 7311-7318
  • Open access: Creative Commons BY license
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    Light and heat control over secondary structure and amyloid-like fiber formation in an overcrowded-alkene-modified Trp zipper

    C. Poloni, M. C. A. Stuart, P. van der Meulen, W. Szymanski and B. L. Feringa, Chem. Sci., 2015, 6, 7311
    DOI: 10.1039/C5SC02735G

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