5-羟甲基糠醛与牛血清白蛋白相互作用的光谱特性研究

目的:研究在模拟人体生理条件下5-羟甲基糠醛(5-HMF)和牛血清白蛋白(BSA)结合反应的特征。方法:采用荧光光谱法和紫外光谱法。取一定浓度的BSA与不同浓度的5-HMF溶液反应(27、37℃下),测定荧光强度和吸光度,再以此通过S理te,r测n-V定ol了m其er公相式互计结算合结时合5-常HM数F和与结B合SA位作点用数距,通离过。计结算果热:2力7、学37数℃据下探5讨-H5M-HFM与FB与SAB的SA结的合相常互数作K用分机别制为;运1.4用×1F0?3rsLt.erm能ol量-1转和移7.9原×103L.mol-1,结合位点数分别为0.61和0.78;根据基本热力学参数判断二者主要通过典型的疏水作用力发生相互作用,作用距离为5.6nm。结论:5-HMF对BSA有较强的荧光猝灭作用,该过程为静态猝灭,二者在试验浓度范围内形成了复合物,从而使5-HMF可以BSA为载体进行贮存和运输。

Spectral Characteristics of Interaction between 5-Hydroxymethyl-2-furaldehyde and Bovine Serum Albumin

OBJECTIVE： To study spectral characteristics of interaction between 5-hydroxymethyl-2-furaldehyde （5-HMF） and bovine serum albumin （BSA） under simulative physiological conditions. METHODS： Spectrofluorimetry and UV spectrophotometry were used. BSA interacted with different concentrations of 5-HMF （at 27℃ or 37 ℃ ） to determine fluorescent intensity and absorbance. The binding constant K and the number of binding sites n were calculated by Stern-Volmer equation, the thermodynamic parameters were used to explore the interaction mechanism of 5-HMF and BSA. The binding distance between BSA and 5-HMF was obtained according to the Forster theory of non-radiation energy. RESULTS： Their binding constant K were 1.4 × 10^3 L. mol^-1 and 7.9×10^3 L.mol^-1, and the number of binding sites n were 0.61 and 0.78, respectively at 27 ℃ and 37 ℃. The thermodynamic parameters indicated that the hydrophobic interaction played a major role in the interaction of 5-HMF with BSA. The binding distance was 5.6 nm between BSA and 5-HMF. CONCLUSION： It shows that the intrinsic fluorescence of BSA was quenched by 5-HMF. The main mechanism of protein fluorescence quenching is a static quenching procedure. 5-HMF could react with BSA to form a complex in the range of experimental concentrations. BSA can be used as carrier for storage and transportation of 5-HME.