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

被引：22

作者：

Argudo, Pablo G. ^{[1
]}

Giner-Casares, Juan J. ^{[2
]}

机构：

[1] Univ Bordeaux, CNRS, Bordeaux INP, LCPO, 16 Ave Pey Berland, F-33600 Pessac, France

[2] Univ Cordoba UCO, Inst Univ Nanoquim IUNAN, Fac Ciencias, Dept Quim Fis & T Aplicada, Campus Rabanales, E-14071 Cordoba, Spain

来源：

NANOSCALE ADVANCES | 2021年 / 3卷 / 07期

关键词：

P. G. A. acknowledges the Région Nouvelle Aquitaine; the Université de Bordeaux; Bordeaux INP and CNRS for financial support. Support from the Ministry of Science and Innovation of Spain through the MANA project CTQ2017-83961-R and JEANS project CTQ2017-92264-EXP is acknowledged. J. J. G.-C. acknowledges the Ministry of Science and Innovation of Spain for a Ramon y Cajal contract (RyC-2014-14956). The Andalusian Government (Consejeria de Economia; Conocimiento; Empresas y Universidades; Junta de Andalucia) of Spain is acknowledged for the financial support through the UCO-1263193 Project;

D O I：

10.1039/d0na00941e

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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.

引用

页码：1789 / 1812

页数：24

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