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

共 179 条

[1] Solution conformational features and interfacial properties of an intrinsically disordered peptide coupled to alkyl chains: a new class of peptide amphiphiles [J].

Accardo, Antonella ;

Leone, Marilisa ;

Tesauro, Diego ;

Aufiero, Rosa ;

Benarouche, Anais ;

Cavalier, Jean-Francois ;

Longhi, Sonia ;

Carriere, Frederic ;

Rossi, Filomena .

MOLECULAR BIOSYSTEMS, 2013, 9 (06) :1401-1410

[2] Molecular Basis for Preventing α-Synuclein Aggregation by a Molecular Tweezer* [J].

Acharya, Srabasti ;

Safaie, Brian M. ;

Wongkongkathep, Piriya ;

Ivanova, Magdalena I. ;

Attar, Aida ;

Klaerner, Frank-Gerrit ;

Schrader, Thomas ;

Loo, Joseph A. ;

Bitan, Gal ;

Lapidus, Lisa J. .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2014, 289 (15) :10727-10737

[3] Dual Self-Assembled Nanostructures from Intrinsically Disordered Protein Polymers with LCST Behavior and Antimicrobial Peptides [J].

Acosta, Sergio ;

Ye, Zhou ;

Aparicio, Conrado ;

Alonso, Matilde ;

Carlos Rodriguez-Cabello, Jose .

BIOMACROMOLECULES, 2020, 21 (10) :4043-4052

[4] Microtubule-Binding R3 Fragment from Tau Self-Assembles into Giant Multistranded Amyloid Ribbons [J].

Adamcik, Jozef ;

Sanchez-Ferrer, Antoni ;

Ait-Bouziad, Nadine ;

Reynolds, Nicholas P. ;

Lashuel, Hilal A. ;

Mezzenga, Raffaele .

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2016, 55 (02) :618-622

[5] 2-DIMENSIONAL SPECTROSCOPY - APPLICATION TO NUCLEAR MAGNETIC-RESONANCE [J].

AUE, WP ;

BARTHOLDI, E ;

ERNST, RR .

JOURNAL OF CHEMICAL PHYSICS, 1976, 64 (05) :2229-2246

[6] Key aromatic/hydrophobic amino acids controlling a cross-amyloid peptide interaction versus amyloid self-assembly [J].

Bakou, Maria ;

Hille, Kathleen ;

Kracklauer, Michael ;

Spanopoulou, Anna ;

Frost, Christina V. ;

Malideli, Eleni ;

Yan, Li-Mei ;

Caporale, Andrea ;

Zacharias, Martin ;

Kapurniotu, Aphrodite .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2017, 292 (35) :14587-14602

[7] HELIX GEOMETRY IN PROTEINS [J].

BARLOW, DJ ;

THORNTON, JM .

JOURNAL OF MOLECULAR BIOLOGY, 1988, 201 (03) :601-619

[8] Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering [J].

Bernado, Pau ;

Svergun, Dmitri I. .

MOLECULAR BIOSYSTEMS, 2012, 8 (01) :151-167

[9] Optimization of the Additive CHARMM All-Atom Protein Force Field Targeting Improved Sampling of the Backbone φ, ψ and Side-Chain χ1 and χ2 Dihedral Angles [J].

Best, Robert B. ;

Zhu, Xiao ;

Shim, Jihyun ;

Lopes, Pedro E. M. ;

Mittal, Jeetain ;

Feig, Michael ;

MacKerell, Alexander D., Jr. .

JOURNAL OF CHEMICAL THEORY AND COMPUTATION, 2012, 8 (09) :3257-3273

[10] Balanced Protein-Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein Association [J].

Best, Robert B. ;

Zheng, Wenwei ;

Mittal, Jeetain .

JOURNAL OF CHEMICAL THEORY AND COMPUTATION, 2014, 10 (11) :5113-5124

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