Protein cage assembly across multiple length scales

被引:132
作者
Aumiller, William M., Jr. [1 ]
Uchida, Masaki [1 ]
Douglas, Trevor [1 ]
机构
[1] Indiana Univ, Dept Chem, Bloomington, IN 47405 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
VIRUS-LIKE PARTICLES; TOBACCO-MOSAIC-VIRUS; COWPEA-CHLOROTIC-MOTTLE; TRANSFER RADICAL POLYMERIZATION; SMALL SPHERICAL VIRUS; HEAT-SHOCK-PROTEIN; ARCHAEOGLOBUS-FULGIDUS FERRITIN; DRUG-DELIVERY APPLICATIONS; SORTASE-MEDIATED LIGATION; P22 SCAFFOLDING PROTEIN;
D O I
10.1039/c7cs00818j
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Within the materials science community, proteins with cage-like architectures are being developed as versatile nanoscale platforms for use in protein nanotechnology. Much effort has been focused on the functionalization of protein cages with biological and non-biological moieties to bring about new properties of not only individual protein cages, but collective bulk-scale assemblies of protein cages. In this review, we report on the current understanding of protein cage assembly, both of the cages themselves from individual subunits, and the assembly of the individual protein cages into higher order structures. We start by discussing the key properties of natural protein cages (for example: size, shape and structure) followed by a review of some of the mechanisms of protein cage assembly and the factors that influence it. We then explore the current approaches for functionalizing protein cages, on the interior or exterior surfaces of the capsids. Lastly, we explore the emerging area of higher order assemblies created from individual protein cages and their potential for new and exciting collective properties.
引用
收藏
页码:3433 / 3469
页数:37
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