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Full Paper
Photochemical Regulation of an Artificial Hydrolase by a Backbone Incorporated Tertiary Structure Switch
Article first published online: 8 DEC 2008
DOI: 10.1002/chem.200801808
Copyright © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Lindgren, N., Varedian, M. and Gogoll, A. (2009), Photochemical Regulation of an Artificial Hydrolase by a Backbone Incorporated Tertiary Structure Switch. Chemistry - A European Journal, 15: 501–505. doi: 10.1002/chem.200801808
Publication History
- Issue published online: 22 DEC 2008
- Article first published online: 8 DEC 2008
- Manuscript Received: 2 SEP 2008
Funded by
- The Swedish Research Council
Keywords:
- aggregation;
- chromophores;
- enzyme catalysis;
- peptidomimetics
Graphical Abstract
Toggling the tertiary structure: Photomodulation of a chromophore in the backbone of a large catalytically active peptide is shown to change the aggregation of the peptide (see figure), thus affecting the rate of hydrolysis of an activated ester.
Abstract
A stilbene chromophore has been incorporated into the turn region of a 42 amino acid peptide, linking two helical peptide sections. Spatial proximity between these sections, as well as aggregation into dimers, is required to facilitate the catalytic function of this artificial hydrolase. Photomodulation of the hydrolase activity results in an increase of the activity of 42 % upon switching from the trans to the cis isomer of the chromophore. This is rationalized by a change in the aggregation state of the peptidomimetic, which is supported by diffusion coefficients obtained from PFG-NMR experiments. The results show that incorporation of a small, relatively flexible chromophore into a large peptide is capable of inducing a considerable change in tertiary structure and thus, functionality.