Issue 6, 2012

Observation of molecular inhibition and binding structures of amyloid peptides

Abstract

Unveiling interactions between labeling molecules and amyloid fibrils is essential to develop new detection methods for studying amyloid structures under various conditions. This review endeavours to reflect the progress in studying interactions between molecular inhibitors and amyloid peptides using a series of experimental approaches, such as X-ray diffraction, nuclear magnetic resonance, scanning probe microscopy, and electron microscopy. The revealed binding mechanisms of anti-amyloid drugs and target proteins could benefit the rational design of drugs for prevention or treatment of amyloidal diseases.

Graphical abstract: Observation of molecular inhibition and binding structures of amyloid peptides

Article information

Article type
Review Article
Submitted
14 Oct 2011
Accepted
17 Jan 2012
First published
14 Feb 2012

Nanoscale, 2012,4, 1895-1909

Observation of molecular inhibition and binding structures of amyloid peptides

C. Wang, A. Yang, X. Li, D. Li, M. Zhang, H. Du, C. Li, Y. Guo, X. Mao, M. Dong, F. Besenbacher, Y. Yang and C. Wang, Nanoscale, 2012, 4, 1895 DOI: 10.1039/C2NR11508E

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