Xiao J B, Chen X Q, Jiang X Y, Hilczer M, Tachiya M
College of Chemistry and Chemical Engineering, Central South University, Changsha, People's Republic of China.
J Fluoresc. 2008 May-Jul;18(3-4):671-8. doi: 10.1007/s10895-008-0346-x. Epub 2008 Mar 20.
The interaction of trans-resveratrol (TRES) and bovine serum albumin (BSA) was investigated using fluorescence spectroscopy (FS) with Tachiya model. The binding number maximum of TRES was determined to be 8.86 at 293.15 K, 23.42 at 303.15 K and 33.94 at 313.15 K and the binding mechanism analyzed in detail. The apparent binding constants (K (a)) between TRES and BSA were 5.02 x 10(4) (293.15 K), 8.89 x 10(4) (303.15 K) and 1.60 x 10(5) L mol(-1) (313.15 K), and the binding distances (r) between TRES and BSA were 2.44, 3.01, and 3.38 nm at 293.15, 303.15, and 313.15 K, respectively. The addition of TRES to BSA solution leads to the enhancement in RLS intensity, exhibiting the formation of the aggregate in solution. The negative entropy change and enthalpy change indicated that the interaction of TRES and BSA was driven mainly by van der Waals interactions and hydrogen bonds. The process of binding was a spontaneous process in which Gibbs free energy change was negative.
采用荧光光谱法（FS）结合立谷模型研究了反式白藜芦醇（TRES）与牛血清白蛋白（BSA）的相互作用。在293.15 K时，TRES的最大结合数为8.86；在303.15 K时为23.42；在313.15 K时为33.94，并对结合机制进行了详细分析。TRES与BSA之间的表观结合常数（Ka）分别为5.02×10⁴（293.15 K）、8.89×10⁴（303.15 K）和1.60×10⁵ L·mol⁻¹（313.15 K），在293.15 K、303.15 K和313.15 K时，TRES与BSA之间的结合距离（r）分别为2.44、3.01和3.38 nm。向BSA溶液中加入TRES会导致共振光散射强度增强，表明溶液中形成了聚集体。负的熵变和焓变表明，TRES与BSA的相互作用主要由范德华相互作用和氢键驱动。结合过程是一个吉布斯自由能变化为负的自发过程。
