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

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 ab...

Full description

Saved in:
Bibliographic Details
Published in:Tetrahedron letters 2008-02, Vol.49 (6), p.987-991
Main Authors: Elgersma, Ronald C., Mulder, Gwenn E., Posthuma, George, Rijkers, Dirk T.S., Liskamp, Rob M.J.
Format: Article
Language:English
Subjects:
Amyloid
Depsipeptide
Peptide nanotubes
Self-assembly
Soft matter
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0040-4039
1873-3581
DOI:10.1016/j.tetlet.2007.12.021