E.G. acknowledge the support of the Israel Science Foundation (ISF).
Amyloids: Not Only Pathological Agents but Also Ordered Nanomaterials†
Article first published online: 15 APR 2008
Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 47, Issue 22, pages 4062–4069, May 19, 2008
How to Cite
Cherny, I. and Gazit, E. (2008), Amyloids: Not Only Pathological Agents but Also Ordered Nanomaterials. Angew. Chem. Int. Ed., 47: 4062–4069. doi: 10.1002/anie.200703133
- Issue published online: 9 MAY 2008
- Article first published online: 15 APR 2008
- Manuscript Received: 13 JUL 2007
- amyloid fibrils;
- materials science;
Amyloid fibers constitute one of the most abundant and important naturally occurring self-associated assemblies. A variety of protein and peptide molecules with various amino acid sequences form these highly stable and well-organized assemblies under diverse conditions. These assemblies display phase states ranging from liquid crystals to rigid nanotubes. The potential applications of these supramolecular assemblies exceed those of synthetic polymers since the building blocks may introduce biological function in addition to mechanical properties. Here we review the structural characteristics of amyloidal supramolecular assemblies, their potential use as either natural or de novo designed sequences, and the range of applications that have been demonstrated so far.