摘要:
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 P-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. (c) 2007 Elsevier Ltd. All rights reserved.