IgG and fibrinogen driven nanoparticle aggregation

作     者：Risto Cukalevski Silvia A. Ferreira Christopher J. Dunning Tord Berggard Tommy Cedervall 

作者机构：Department of Biochemistry and Structural Biology Centre for Molecular Protein Science Chemical Centre Lund University PO Box 124 SE-22100 Lund Sweden Centre for Biological Engineering University of Minho Campus Gualtar 4710-057 Braga Portugal Neuronal Survival Unit Department of Experimental Medical Science Wallenberg Neuroscience Center Lund University BMC B 11 22184 Lund Sweden Alligator Bioscience AB Lund Sweden 

出 版 物：《Nano Research》 (纳米研究（英文版）)

年 卷 期：2015年第8卷第8期

页      面：2733-2743页

核心收录：

学科分类：1007[医学-药学(可授医学、理学学位)] 100705[医学-微生物与生化药学] 0808[工学-电气工程] 0809[工学-电子科学与技术（可授工学、理学学位）] 07[理学] 070205[理学-凝聚态物理] 08[工学] 080501[工学-材料物理与化学] 0805[工学-材料科学与工程（可授工学、理学学位）] 0702[理学-物理学] 10[医学] 

基　　金：Nanometer structure consortium at Lund University (nmC@LU) Lars Hierta Foundation research school FLAK of Lund University 

主　　题：nanoparticles(NPs) protein coron aggregation immunoglobulin 

摘      要：A thorough understanding of how proteins induce nanoparticle （NP） aggregation is crucial when designing in vitro and in vivo assays and interpreting experimental results. This knowledge is also crucial when developing nano-applications and formulation for drug delivery systems. In this study, we found that extraction of immunoglobulin G （IgG） from cow serum results in lower polystyrene NPs aggregation. Moreover, addition of isolated IgG or fibrinogen to fetal cow serum enhanced this aggregation, thus demonstrating that these factors are major drivers of NP aggregation in serum. Counter-intuitively, NP aggregation was inversely dependent on protein concentration; i.e., low protein concentrations induced large aggregates, whereas high protein concentrations induced small aggregates. Protein-induced NP aggregation and aggregate size were monitored by absorbance at 400 nm and dynamic light scattering, respectively. Here, we propose a mechanism behind the protein concentration dependent aggregation; this mechanism involves the effects of multiple protein interactions on the NP surface, surface area limitations, aggregation kinetics, and the influence of other serum proteins.