Effects of gene carrier polyethyleneimines on the structure and binding capability of bovine serum albumin

被引:21
作者
Guo, Zhiyong [1 ]
Kong, Zhijie [1 ]
Wei, Yanshan [1 ]
Li, Hua [1 ]
Wang, Yajing [1 ]
Huang, Aimin [1 ]
Ma, Lin [1 ]
机构
[1] Guangxi Univ, Sch Chem & Chem Engn, Nanning 530004, Peoples R China
基金
中国国家自然科学基金;
关键词
Polyethyleneimine; Bovine serum albumin; Conformation; Interaction; Binding; PROTEIN INTERACTION; CIRCULAR-DICHROISM; FLUORESCENCE; THERAPY; SPECTROSCOPY; QUERCETIN; DELIVERY; POLYETHYLENIMINE; HYDROXYFLAVONES; POLYELECTROLYTE;
D O I
10.1016/j.saa.2016.10.026
中图分类号
O433 [光谱学];
学科分类号
0703 ; 070302 ;
摘要
Polyethyleneimine (PEI), one of the most effective non-viral gene carriers, is also cytotoxic, however the molecular basis is poorly understood. Little is known about the effects of PEI on the structure and functions of the biomacromolecules. In this work, fluorescence, UV-vis absorption, circular dichroism (CD) spectroscopy and zeta-potential measurement were conducted to reveal the interaction between PEIs (average molecular weight 25,10 and 1.8 kDa) and bovine serum albumin (BSA), and to evaluate the effects on the conformation of BSA as long as its binding capability to the model compounds, 8-anilino-1-naphthalenesulfonic acid (ANS) and quercetin. PEIs were found to complex with BSA and induced a conformational change of the protein by a major reduction of alpha-helix at PEI concentration <0.2 mg.mL(-1) and an increase at higher PEI concentration. The binding efficacy of ANS and quercetin to BSA was greatly reduced by the competitive binding by PEI and influenced by the conformational change of BSA, which was found to display a similar trend to the change of the alpha-helix content of the protein. The polymer size played an important role in PEI-BSA interaction. PEI of higher molecular weight was more favorable to interact with BSA and more efficient to perturb the conformation and binding capability of the protein. (C) 2016 Elsevier B.V. All rights reserved.
引用
收藏
页码:783 / 791
页数:9
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