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Solvent-induced conformational changes in cyclic peptides: a vibrational circular dichroism study

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Bravo-Rodriguez,  Kenny
Research Group Sánchez-García, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Sanchez-Garcia,  Elsa
Research Group Sánchez-García, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Citation

Merten, C., Li, F., Bravo-Rodriguez, K., Sanchez-Garcia, E., Xu, Y., & Sander, W. (2014). Solvent-induced conformational changes in cyclic peptides: a vibrational circular dichroism study. Physical Chemistry Chemical Physics, 16(12), 5627-5633. doi:10.1039/C3CP55018D.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-DA67-F
Abstract
The three-dimensional structure of a peptide is strongly influenced by its solvent environment. In the present study, we study three cyclic tetrapeptides which serve as model peptides for β-turns. They are of the general structure cyclo(Boc-Cys-Pro-X-Cys-OMe) with the amino acid X being either glycine (1), or L- or D-leucine (L- or D-2). Using vibrational circular dichroism (VCD) spectroscopy, we confirm previous NMR results which showed that D-2 adopts predominantly a βII turn structure in apolar and polar solvents. Our results for L-2 indicate a preference for a βI structure over βII. With increasing solvent polarity, the preference for 1 is shifted from bII towards βI. This conformational change goes along with the breaking of an intramolecular hydrogen bond which stabilizes the βII conformation. Instead, a hydrogen bond with a solvent molecule can stabilize the βI turn conformation.