Peptide self-assembly: from toxins to amyloid fibrils and nanotubes.
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.
Anoop
A
Rawat
CSIR-Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India. nraj@ccmb.res.in.
Ramakrishnan
R
Nagaraj
D000682:Amyloid / Q000737:chemistry*; D043942:Nanotubes / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D014118:Toxins, Biological / Q000737:chemistry*
D000682:Amyloid; D010455:Peptides; D014118:Toxins, Biological