On the role of surface composition and curvature on biointerface formation and colloidal stability of nanoparticles in a protein-rich model system

被引:38
作者
Orts-Gil, Guillermo [1 ]
Natte, Kishore [1 ]
Thiermann, Raphael [2 ]
Girod, Matthias [2 ]
Rades, Steffi [3 ]
Kalbe, Henryk [3 ]
Thuenemann, Andreas F. [2 ]
Maskos, Michael [4 ]
Oesterle, Werner [1 ]
机构
[1] Fed Inst Mat Res & Testing BAM 5 1, D-12205 Berlin, Germany
[2] BAM Fed Inst Mat Res & Testing BAM 6 5, D-12489 Berlin, Germany
[3] BAM Fed Inst Mat Res & Testing BAM 6 8, D-12203 Berlin, Germany
[4] IMM, D-55129 Mainz, Germany
关键词
Nanoparticles; Protein corona; Biointerface; BSA; PEG; Colloidal stability; INTENSITY CORRELATION SPECTROSCOPY; BOVINE SERUM-ALBUMIN; SILICA NANOPARTICLES; SPHERICAL-PARTICLES; OXIDE NANOPARTICLES; CORONA; SIZE; AGGREGATION; LYSOZYME; INTERNALIZATION;
D O I
10.1016/j.colsurfb.2013.02.027
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
The need for a better understanding of nanoparticle-protein interactions and the mechanisms governing the resulting colloidal stability has been emphasised in recent years. In the present contribution, the short and long term colloidal stability of silica nanoparticles (SNPs) and silica-poly(ethylene glycol) nanohybrids (Sil-PEG) have been scrutinised in a protein model system. Well-defined silica nanoparticles are rapidly covered by bovine serum albumin (BSA) and form small clusters after 20 min while large agglomerates are detected after 10 h depending on both particle size and nanoparticle-protein ratio. Oppositely, Sil-PEG hybrids present suppressive protein adsorption and enhanced short and long term colloidal stability in protein solution. No critical agglomeration was found for either system in the absence of protein, proving that instability found for SNPs must arise as a consequence of protein adsorption and not to high ionic environment. Analysis of the small angle X-ray scattering (SAXS) structure factor indicates a short-range attractive potential between particles in the silica-BSA system, which is in good agreement with a protein bridging agglomeration mechanism. The results presented here point out the importance of the nanoparticle surface properties on the ability to adsorb proteins and how the induced or depressed adsorption may potentially drive the resulting colloidal stability. (c) 2013 Elsevier B.V. All rights reserved.
引用
收藏
页码:110 / 119
页数:10
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