Spectroscopic investigation of the interactions between gold nanoparticles and bovine serum albumin

• 来源期刊: 科学通报(英文版)
• 学科: 工学
• 年，卷（期）: 2012,（10）
• 页码范围: 1109-1115
• 页数: 7页
• 分类号: TB383.1
• 语种: 中文

摘要

The interactions between bovine serum albumin(BSA) and gold nanoparticles(AuNPs) ,and the conformational changes of BSA induced by this interaction,were investigated by UV-visible absorption spectroscopy,fluorescence spectroscopy,and Fourier transform infrared in combination with attenuated total reflection spectroscopy(ATR-FTIR) .The critical adsorption density for preventing AuNP aggregation in 0.1 mol/L phosphate buffered saline(pH 7.2) was 23 BSA molecules per gold particle or 3.8*1012 BSA molecules/cm2.BSA bound to the AuNPs with high affinity(binding constant Ks=7.59*108 L/mol) ,and the intrin-sic fluorescence of BSA was quenched by the AuNPs in accordance with the static quenching mechanism.Both fluorescence spectroscopy and ATR-FTIR showed that AuNPs induced conformational changes in BSA,which resulted in it becoming less compact and increased the polarity of the microenvironment around the tryptophan residue Trp-212.