Peptide Self-assembly: From Toxins to Amyloid Fibrils and Nanotubes
Anoop Rawat and Ramakrishnan Nagaraj
Pages 740-746 (7)
The process of self-assembly is universal and lies at the heart of biological structures and function. Peptide aggregation,
while considered a nuisance in peptide chemistry, soon gained interest with the discovery of pore-forming peptide
toxins and had been an area of intense research during last century and even to date. This has also resulted in the increasing
use of the more respectable term peptide self-assembly. The discovery of amyloid forming peptides has rekindled
the interest in peptide self-assembly since such aggregates are directly implicated in many debilitating diseases in human
and animals. Amyloid aggregates have posed many fundamental questions to researchers. In addition, self-assembly of
peptides has emerged as a bottom-up strategy for the fabrication of nanostructures owing to highly ordered nature of the
process and considerable degree of flexibility and diversity provided by peptides as starting materials. This review provides
a brief account of the progress in the field of peptide self-assembly from pore-forming toxins to amyloid forming
peptides and those forming nanostructures.
Aβ peptides, amyloids, nanostructures, peptide channels, peptide toxins, peptide self-assembly.
CSIR-Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India.