The interaction between flower-like CdSe nanostructure particles (CdSe NP) and bovine serum albumin (BSA) was investigated from a spectroscopic angle under simulative physiological conditions. Under pH 7.4, CdSe NP could effectively quench the intrinsic fluorescence of BSA via static quenching. The binding constant (K_A) was 6.38, 3.27, and 1.90×10~4 M ~(-1) at 298, 304, and 310 K, respectively and the number of binding sites was 1.20. According to the Vant Hoff equation, the thermodynamic parameters (ΔH°=-77.48 kJ mol~(-1), ΔS°=-168.17 J mol~(-1) K~(-1)) indicated that hydrogen bonds and van der Waals forces played a major role in stabilizing the BSA-CdSe complex. Besides, UVvis and circular dichroism (CD) results showed that the addition of CdSe NP changed the secondary structure of BSA and led to a decrease in α-helix. These results suggested that BSA underwent substantial conformational changes induced by flower-like CdSe nanostructure particles.
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