文摘
The understanding of the protein-nanoclusters interaction has significant implications for biological applications of nanoclusters (NCs). In this manuscript, the interaction of histidine-capped Au nanoclusters (NCs) with bovine serum albumin (BSA) has been investigated by fluorescence, UV-vis, circular dichroism (CD) and Raman spectroscopic techniques under simulative physiological conditions. The results showed that the fluorescence of BSA was quenched by Au NCs. The quenching mechanism was discussed to be a dynamic quenching style, which was proved by the fluorescence spectra and UV-vis absorption spectra. According to modified Stern-Volmer equations at different temperatures, corresponding thermodynamic parameters, 螖H胃, 螖S胃 and 螖G胃 were observed to be 35.97 kJ mol鈭?, 199.53 J mol鈭? K鈭? and 鈭?3.49 kJ mol鈭?, respectively. The hydrophobic force played a key role in the interaction process. Further results from the CD spectra and Raman spectra demonstrated that the 伪-helical content in BSA was reduced upon interaction with Au NCs which induced a partial protein destabilization. This study contributes to a better understanding of the biology toxicity of Au NCs to biomolecular, which is very essential for the development of safe and functional Au NCs.