本文選題：光譜法 + 分子模擬��； 參考：《光譜學與光譜分析》2017年08期

【摘要】：采用多種光譜技術結合圓二色譜技術研究了考馬斯亮藍G-250(CBBG-250)相互作用于牛血清白蛋白(BSA),探究了兩者之間的作用機理。熒光光譜結果表明BSA與CBBG-250結合形式是靜態(tài)猝滅,隨CBBG-250濃度增加,其形成常數(shù)隨溫度逐漸減小,結合比為1∶1,根據(jù)Stern-Volmer曲線計算焓變值(ΔH)和熵變值(ΔS)分別為-4.38kJ·mol~(-1)和-6.16J·mol~(-1)·K~(-1),均小于零,證明該過程是一個自發(fā)過程。傅里葉紅外光譜測定結果表明CBBG-250的加入引起B(yǎng)SA結構的變化,隨著CBBG-250溶液濃度的增加,BSA中色氨酸微環(huán)境極性被改變,在1 600~1 700cm~(-1)(酰胺帶Ⅰ)和1 600~1 500cm~(-1)(酰胺帶Ⅱ)處的特征吸收帶藍移。其中1 650cm~(-1)移動至1 710cm~(-1),1 544cm~(-1)移動到1 573cm~(-1),顯示BSAα-螺旋(1 650~1 658cm~(-1))和β-折疊(1 620~1 640cm~(-1),1 675cm~(-1))結構發(fā)生變化,且α-螺旋含量比結合前有所降低。圓二色譜分析結果表明,兩者間通過氫鍵和范德華力為主的作用力使得BSA二級結構發(fā)生變化,α-螺旋含量由42.15%下降至1.27%,該結果進一步被分子建模對接技術證明。
[Abstract]:The interaction between Coomassie brilliant blue G-250 (CBBG-250) and bovine serum albumin (BSA) was studied by means of multiple spectral techniques and circular dichroism. The fluorescence spectra show that the binding form of BSA and CBBG-250 is static quenching. With the increase of CBBG-250 concentration, the formation constant decreases gradually with the temperature and the binding ratio is 1: 1. The calculated values of enthalpy variation (螖 H) and entropy variation (螖 S) based on Stern-Volmer curve are -4.38 kJ / mol ~ (-1) and -6.16 J / mol ~ (-1) K ~ (-1), respectively, which are less than zero. It is proved that this process is a spontaneous process. The results of Fourier transform infrared spectroscopy showed that the addition of CBBG-250 caused the change of BSA structure, and the microenvironmental polarity of tryptophan in BSA changed with the increase of CBBG-250 solution concentration. The blue shift of the absorption band is observed at 1 600 ~ 1 700 cm ~ (-1) (amide band 鈪，

本文編號：2001214