Protein-silver nanoparticle interactions to colloidal stability in acidic environments

Jui Ting Tai, Chao Shun Lai, Hsin Chia Ho, Yu Shan Yeh, Hsiao Fang Wang, Rong Ming Ho, De Hao Tsai

研究成果: Article査読

49 被引用数 (Scopus)

抄録

We report a kinetic study of Ag nanoparticles (AgNPs) under acidic environments (i.e., pH 2.3 to pH ≈7) and systematically investigate the impact of protein interactions [i.e., bovine serum albumin (BSA) as representative] to the colloidal stability of AgNPs. Electrospray-differential mobility analysis (ES-DMA) was used to characterize the particle size distributions and the number concentrations of AgNPs. Transmission electron microscopy was employed orthogonally to provide visualization of AgNPs. For unconjugated AgNPs, the extent of aggregation, or the average particle size, was shown to be increased significantly with an increase of acidity, where a partial coalescence was found between the primary particles of unconjugated AgNP clusters. Aggregation rate constant, kD, was also shown to be proportional to acidity, following a correlation of log(kD) = 1.627(pH)-9.3715. Using ES-DMA, we observe BSA had a strong binding affinity (equilibrium binding constant, ≈ 1.1 × 106 L/mol) to the surface of AgNPs, with an estimated maximum molecular surface density of ≈0.012 nm-2. BSA-functionalized AgNPs exhibited highly-improved colloidal stability compared to the unconjugated AgNPs under acidic environments, where both the acid-induced interfacial dissolution and the particle aggregation became negligible. Results confirm a complex mechanism of colloidal stability of AgNPs: the aggregation process was shown to be dominant, and the formation of BSA corona on AgNPs suppressed both particle aggregation and interfacial dissolution of AgNP samples under acidic environments.

本文言語English
ページ(範囲)12755-12764
ページ数10
ジャーナルLangmuir
30
43
DOI
出版ステータスPublished - 2014 11 4
外部発表はい

ASJC Scopus subject areas

  • 材料科学(全般)
  • 凝縮系物理学
  • 表面および界面
  • 分光学
  • 電気化学

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