Abstract
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 K s=7.59×108 L/mol), and the intrinsic 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.
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Shi, X., Li, D., Xie, J. et al. Spectroscopic investigation of the interactions between gold nanoparticles and bovine serum albumin. Chin. Sci. Bull. 57, 1109–1115 (2012). https://doi.org/10.1007/s11434-011-4741-3
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DOI: https://doi.org/10.1007/s11434-011-4741-3