A protein-protein host-guest complex: Thermostable ferritin encapsulating positively supercharged green fluorescent protein

被引：18

作者：

Pulsipher, Katherine W. ^{[1
]}

Bulos, Joshua A. ^{[1
]}

Villegas, Jose A. ^{[1
]}

Saven, Jeffery G. ^{[1
]}

Dmochowski, Ivan J. ^{[1
]}

机构：

[1] Univ Penn, Dept Chem, Philadelphia, PA 19104 USA

来源：

PROTEIN SCIENCE | 2018年 / 27卷 / 10期

基金：

美国国家科学基金会;

关键词：

ferritin; encapsulation; protein-protein interactions; supercharged protein; host-guest interactions; ARCHAEOGLOBUS-FULGIDUS; BACTERIOPHAGE P22; MAMMALIAN-CELLS; IN-VITRO; DRUG; NANOPARTICLES; INTERFACE; CONTAINER; CAGES; ASSEMBLIES;

D O I：

10.1002/pro.3483

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We characterize the encapsulation of supercharged green fluorescent protein, GFP(+36), by thermophilic ferritin from Archaeoglobus fulgidus (AfFtn). The AfFtn-GFP(+36) assembly is rapid, nearly stoichiometric, and robust. Using a more stably assembled mutant AfFtn, we show that encapsulation can occur in the presence of mostly assembled cages, in addition to encapsulation starting from AfFtn individual subunits. Assembly and encapsulation do not occur with non-supercharged GFP or the alternately supercharged GFP(-30), highlighting the role of complementary electrostatic interactions between the cargo and AfFtn cage interior. We also present a method for verifying protein-protein encapsulation, using nickel nitrilotriacetic acid agarose resin. AfFtn-supercharged protein host-guest complexes could find applications in enzyme studies, protein separations, and in vivo protein stabilization and targeted delivery.

引用

页码：1755 / 1766

页数：12

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