中文摘要：

在牛的浆液白朊(BSA ) 和金 nanoparticles (AuNPs ) 之间的相互作用，和 BSA 的 conformational 变化由这个相互作用导致了，被紫外可见的吸收光谱学，荧光光谱学，和在联合红外线的 Fourier 变换与稀释全部的思考光谱学(ATR-FTIR ) 调查。为在 0.1 mol/L 磷酸盐阻止 AuNP 聚集的批评吸附密度缓冲了盐( pH 7.2 )每金粒子是 23 个 BSA 分子或 3.8 ??挠浯楢敮?楷桴琠敨愠慮祬楳?景瘠汯慴敧琭浩?敲灳湯敳?畤楲杮?佁瀠潲散獳?敔瑳漠?敷杩?氠獯?慷?潣摮'渍?瑡愠??‥慎汃猠汯瑵潩?潴愠獳獥?桴?敲楳瑳湡散琠?潣牲獯潩?吠敨爠獥汵獴椠摮捩瑡?桴瑡琠敨挠牵敲瑮搠湥楳祴愠摮搠瑵?祣汣?汰祡欠祥爠汯獥漠?桴?潣瑡湩?畱污瑩?吠敨瀠慥?潶瑬条?畤楲杮?佁瀠潲散獳椠据敲獡摥眠瑩?桴?湩牣慥敳椠?畣牲湥?敤獮瑩?畢?桴?潣瑡湩?潷汵?敢洠牯? 慥楳

英文摘要：

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 3.8x 1012 B SA molecules/cm2. B SA bound to the AuNPs with high affinity （binding constant Ks= 7.59×10^8 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.