Issue 1, 2015

Supramolecular chirality in peptide microcrystals

Abstract

The vibrational circular dichroism (VCD) spectra of microcrystals of fibril-forming peptides have been measured for the first time. VCD spectra were measured and compared for microcrystals and fibrils formed from the same peptide, human islet amyloid polypeptide (IAPP, amylin). Structural information related to the supramolecular chirality of both the microcrystals and the fibrils, as well as the VCD enhancement mechanisms in fibrils and microcrystals, is obtained from these spectral comparisons. It is concluded that strongly enhanced VCD does not require braiding of two or more filaments that is permitted in fibrils but not microcrystals.

Graphical abstract: Supramolecular chirality in peptide microcrystals

Supplementary files

Article information

Article type
Communication
Submitted
30 Jun 2014
Accepted
17 Oct 2014
First published
20 Oct 2014

Chem. Commun., 2015,51, 89-92

Author version available

Supramolecular chirality in peptide microcrystals

D. Kurouski, J. D. Handen, R. K. Dukor, L. A. Nafie and I. K. Lednev, Chem. Commun., 2015, 51, 89 DOI: 10.1039/C4CC05002A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements