摘要
采用荧光光谱法研究氧化石墨烯纳米粒(N GO)对牛血清白蛋白(BSA)的作用机制。实验结果表明:NGO对BSA的荧光猝灭类型为动态猝灭为主的静动态混合猝灭。T=283、298、310K时,二者最小结合常数分别为6.7×109、9.5×107、2.1×106L mol-1。结合位点数分别为2.12、1.32、0.87。由热力学参数确定N G O与BSA之间作用类型为氢键和范德华力。N GO对BSA中色氨酸残基荧光猝灭,不改变酪氨酸残基荧光发射强度,但降低其所处环境的疏水性。
The interaction mechanism serum albumin （BSA） was studied by between nanoscale grapheme oxide （NGO） and bovine fluorescence spectroscopy. The fluorescence quenching mechanism between NGO and BSA was determined as mainly dynamic quenching, combined with static quenching. The minimum binding constants between NGO and BSA were 6.7×109、9.5×107、2.1×106L·mol-1 at 283,298 and 310K while the numbers of binding sites were 2.12,1.32,0.87. According to the thermodynamic parameters,the interaction between NGO and BSA was driven by n-n interaction and hydrophobic interaction. The fluorescence intensity of tryptophan residue in BSA was quenched by NGO. The synchronous fluorescence spectral results indicated that the hydrophobicity of tyrosine residue reduced while the microenvironment around tryptophan residue had no change.
出处
《光谱实验室》
CAS
2013年第5期2235-2241,共7页
Chinese Journal of Spectroscopy Laboratory
基金
重庆市卫生局面上项目(No.2012-2-167)
重庆市高校微纳米材料工程与技术重点实验室资助项目(No.KFJJ1208)
重庆医科大学附属永川医院资助重点项目(No.YJZD20120006)
关键词
氧化石墨烯纳米粒
牛血清白蛋白
荧光光谱法
Nanoscale Graphene Oxide
Bovine Serum Albumin
Fluorescence Spectroscopy
