摘要
用 U V- vis光谱和表面增强拉曼光谱研究了稀土离子和牛血清白蛋白 (BSA)的作用。紫外光谱研究表明 ,Ce4 + 、Er3+ 离子能配位诱导 BSA,使其分子中色氨酸和酪氨酸芳杂环疏水基团外露 ,2 80 nm处的吸收强度增大。当固定 BSA∶ Ce4 + 摩尔比为 1∶ 2时 ,随 BSA浓度增大 ,Ce4 + 离子配位诱导使 BSA构象发生变化 ,α-螺旋含量减少 ,致使 2 30 nm吸收峰红移 ,2 80 nm吸收峰强度增大幅度比 2 30 nm处大。拉曼光谱研究表明 ,Ce4 + 离子很可能和肽键上的 C=O基及边链羧基上的 C=O基都发生配位作用 ,并引起 BSA肽链伸展。
The interaction of rare earth ions with bovine serum albumin(BSA)has been studied by UV spectrometry and surface enhanced raman scattering (SERS)spectrometry Ultraviolet spectra show that the hydrophobic residues of tryptophane and tyrosine are exposed and the adsorption intensity at 280nm is increased because of the coordination of Ce 4+ ,Er 3+ ions with BSA Fixing the molar ratio of BSA to Ce 4+ 1∶2,with the increasing of the concentration of BSA,the conformation of BSA changes because of the induction of Ce 4+ ion,α-helix content decreases,the adsorption peak at 230nm moves towards long wavelength,and the adsorption intensity increases faster at 280nm than at 230nm SERS spectra show that Ce 4+ ion is likely to coordinate with C=O coming from peptide bonds and side-chain carboxyl groups,and leads to the stretch of peptide chain of BSA
出处
《稀土》
EI
CAS
CSCD
北大核心
2002年第5期22-25,共4页
Chinese Rare Earths
基金
上海市自然科学基金 (0 0 ZA14 0 42 )资助
