Protein Identity and Environmental Parameters Determine the Final Physicochemical Properties of Protein-Coated Metal Nanoparticles

被引:33
作者
Dewald, Inna [1 ]
Isakin, Olga [1 ]
Schubert, Jonas [1 ,4 ]
Kraus, Tobias [2 ]
Chanana, Munish [1 ,3 ]
机构
[1] Univ Bayreuth, Phys Chem 2, D-95447 Bayreuth, Germany
[2] Leibniz Inst New Mat, INM, D-66123 Saarbrucken, Germany
[3] ETH, Inst Bldg Mat IfB, CH-8093 Zurich, Switzerland
[4] Leibniz Inst Polymer Res Dresden, D-01069 Dresden, Germany
关键词
AMINO-ACID-SEQUENCE; GOLD NANOPARTICLES; ISOELECTRIC POINTS; SILICA NANOPARTICLES; MOLECULAR-WEIGHTS; IONIC-STRENGTH; PORCINE PEPSIN; BINDING; LYSOZYME; AGGREGATION;
D O I
10.1021/acs.jpcc.5b06266
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
When a nanomaterial enters a biological system, proteins adsorb onto the particle surface and alter the surface properties of nanoparticles, causing drastic changes in physicochemical properties such as hydrodynamic size, surface charge and aggregation state, thus giving a completely new and undefined physicochemical identity to the nanoparticles. In the present work, we study the impact of the protein identity (molecular weight and isoelectric point) and the environmental conditions (pH and ionic strength) on the final physicochemical properties of a model nanoparticle system, i.e. gold nanoparticles. Gold nanoparticles either form stable dispersions or agglomerate spontaneously when mixed with protein solutions, depending on the protein and the experimental conditions. Strikingly, the agglomerates redisperse to individually dispersed and colloidally stable nanoparticles, depending on the purification pH. The final protein coated nanoparticles exhibit specific stabilities and surface charges that depend on protein type and the conditions during its adsorption. By understanding the interactions of nanoparticles with proteins under controlled conditions, we can define the protein corona of the nanoparticles and thus their physicochemical properties in various media.
引用
收藏
页码:25482 / 25492
页数:11
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