Mirror image supramolecular helical tapes formed by the enantiomeric-depsipeptide derivatives of the amyloidogenic peptide amylin(20–29)

Elgersma, R.C., Mulder, G.E., Posthuma, G., Rijkers, D.T.S. and Liskamp, R.M.J. (2008) Mirror image supramolecular helical tapes formed by the enantiomeric-depsipeptide derivatives of the amyloidogenic peptide amylin(20–29). Tetrahedron Letters, 49(6), pp. 987-991. (doi:10.1016/j.tetlet.2007.12.021)

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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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Liskamp, Professor Robert
Authors: Elgersma, R.C., Mulder, G.E., Posthuma, G., Rijkers, D.T.S., and Liskamp, R.M.J.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Tetrahedron Letters
ISSN:0040-4039
ISSN (Online):1873-3581

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