In Silico Evidence That Protein Unfolding is a Precursor of Protein Aggregation

被引：17

作者：

Bianco, Valentino ^{[1
]}

Franzese, Giancarlo ^{[2
,3
]}

Coluzza, Ivan ^{[4
,5
]}

机构：

[1] Univ Complutense Madrid, Fac Chem, Dept Chem Phys, Plaza Ciencias,Ciudad Univ, E-28040 Madrid, Spain

[2] Univ Barcelona, Fac Fis, Seccio Fis Estadist & Interdisciplinaria, Dept Fis Mat Condensada, Marti i Franques 1, E-08028 Barcelona, Spain

[3] Univ Barcelona, Inst Nanosci & Nanotechnol IN2UB, Marti i Franques 1, E-08028 Barcelona, Spain

[4] CIC biomaGUNE, Paseo Miramon 182, San Sebastian 20014, Spain

[5] Basque Fdn Sci, Ikerbasque, Bilbao 48013, Spain

来源：

CHEMPHYSCHEM | 2020年 / 21卷 / 05期

基金：

奥地利科学基金会;

关键词：

aqueous environments; computational chemistry; hydration shell; protein aggregation; protein folding; HYDROPHOBIC HYDRATION; LATTICE MODELS; WATER; STABILITY; STATE; COLD; INTERMEDIATE; SIMULATIONS; TEMPERATURE; DYNAMICS;

D O I：

10.1002/cphc.201900904

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

We present a computational study on the folding and aggregation of proteins in an aqueous environment, as a function of its concentration. We show how the increase of the concentration of individual protein species can induce a partial unfolding of the native conformation without the occurrence of aggregates. A further increment of the protein concentration results in the complete loss of the folded structures and induces the formation of protein aggregates. We discuss the effect of the protein interface on the water fluctuations in the protein hydration shell and their relevance in the protein-protein interaction.

引用

页码：377 / 384

页数：8

共 85 条

[1] A Simple Lattice Model That Captures Protein Folding, Aggregation and Amyloid Formation [J].