| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5275485 | Tetrahedron Letters | 2008 | 5 Pages |
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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Authors
Ronald C. Elgersma, Gwenn E. Mulder, George Posthuma, Dirk T.S. Rijkers, Rob M.J. Liskamp,