Alcohol-perturbed self-assembly of the tobacco mosaic virus coat protein

被引：3
作者：
Abu-Baker, Ismael [1 ]
Blum, Amy Szuchmacher [1 ]
机构：
[1] McGill Univ, Dept Chem, Montreal, PQ, Canada
来源：
BEILSTEIN JOURNAL OF NANOTECHNOLOGY | 2022年 / 13卷
基金：
加拿大创新基金会; 加拿大自然科学与工程研究理事会;
关键词：
alcohol; hydrophobic effect; protein assembly; self-assembly; tobacco mosaic virus; STACKED-DISK AGGREGATE; ETHANOL; MIXTURES; DYNAMICS; PARTICLE;
D O I：
10.3762/bjnano.13.30
中图分类号：
TB3 [工程材料学];
学科分类号：
0805 ; 080502 ;
摘要：
The self-assembly of the tobacco mosaic virus coat protein is significantly altered in alcohol-water mixtures. Alcohol cosolvents stabilize the disk aggregate and prevent the formation of helical rods at low pH. A high alcohol content favours stacked disk assemblies and large rafts, while a low alcohol concentration favours individual disks and short stacks. These effects appear to be caused by the hydrophobicity of the alcohol additive, with isopropyl alcohol having the strongest effect and methanol the weakest. We discuss several effects that may contribute to preventing the protein-protein interactions between disks that are necessary to form helical rods.
引用
收藏
页码：355 / 362
页数：8
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