Mirror image supramolecular helical tapes formed by the enantiomeric-depsipeptide derivatives of the amyloidogenic peptide amylin(20-29) |
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| Authors: | Ronald C. Elgersma George Posthuma Rob M.J. Liskamp |
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| Affiliation: | a Medicinal Chemistry and Chemical Biology, Utrecht Institute for Pharmaceutical Sciences, Department of Pharmaceutical Sciences, Faculty of Science, Utrecht University, PO Box 80082, 3508 TB Utrecht, The Netherlands
b Department of Cell Biology, Center for Electron Microscopy, University Medical Center, 3508 GA Utrecht, The Netherlands |
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| Abstract: | Factors that determine the chirality of supramolecular helical tapes formed by a backbone-modified amylin(20-29) depsipeptide and inverso-depsipeptide, were studied by Fourier transform infrared spectroscopy, circular dichroism and transmission electron microscopy. Although β-sheet propensity was absent in both peptides, it was found that the l-depsipeptide formed left-handed and the enantiomeric d-depsipeptide right-handed helical tapes. Moreover, the backbone-modified depsipeptides, showed a certain degree of cross-recognition between both enantiomers, which might have implications in designing amyloid formation inhibitors. |
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| Keywords: | Amyloid Depsipeptide Peptide nanotubes Self-assembly Soft matter |
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