Issue 7, 2021

Folding and self-assembly of short intrinsically disordered peptides and protein regions

Abstract

Proteins and peptide fragments are highly relevant building blocks in self-assembly for nanostructures with plenty of applications. Intrinsically disordered proteins (IDPs) and protein regions (IDRs) are defined by the absence of a well-defined secondary structure, yet IDPs/IDRs show a significant biological activity. Experimental techniques and computational modelling procedures for the characterization of IDPs/IDRs are discussed. Directed self-assembly of IDPs/IDRs allows reaching a large variety of nanostructures. Hybrid materials based on the derivatives of IDPs/IDRs show a promising performance as alternative biocides and nanodrugs. Cell mimicking, in vivo compartmentalization, and bone regeneration are demonstrated for IDPs/IDRs in biotechnological applications. The exciting possibilities of IDPs/IDRs in nanotechnology with relevant biological applications are shown.

Graphical abstract: Folding and self-assembly of short intrinsically disordered peptides and protein regions

Article information

Article type
Review Article
Submitted
10 Nov 2020
Accepted
17 Jan 2021
First published
18 Jan 2021
This article is Open Access
Creative Commons BY-NC license

Nanoscale Adv., 2021,3, 1789-1812

Folding and self-assembly of short intrinsically disordered peptides and protein regions

P. G. Argudo and J. J. Giner-Casares, Nanoscale Adv., 2021, 3, 1789 DOI: 10.1039/D0NA00941E

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