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机构地区:[1]南昌大学食品科学与技术国家重点实验室,江西南昌330047 [2]南昌大学化学系,江西南昌330031
出 处:《化学研究与应用》2013年第12期1680-1685,共6页Chemical Research and Application
基 金:国家自然科学基金项目(21065007)资助;南昌大学食品科学与技术国家重点实验室基金(SKLF-ZZA-201302;SKLF-ZZB-201303)资助
摘 要:在模拟生理(pH=7.4)条件下,运用荧光光谱研究Ag纳米粒子存在时,尼古丁与牛血清白蛋白(BSA)的相互作用。结果表明不存在Ag纳米粒子时,尼古丁能静态猝灭BSA的固有荧光,且结合力主要是氢键和范德华力;而Ag纳米粒子的存在能降低尼古丁对BSA作用的猝灭常数和结合常数。为了分析Ag纳米抑制尼古丁与BSA作用的原因,本工作将同步荧光光谱、红外光谱以及圆二色谱用于Ag纳米粒子与BSA相互作用的研究,结果表明Ag纳米粒子与BSA的结合会引发BSA二级结构的改变。The binding interaction of Nicotine to bovine serum albumin (BSA) in presence of AgNPs was studied by spectrometry under simulated physiological conditions. The fluorescence spectra of BSA with Nicotine were recorded at 298K, 302K and 306 K, which were used to evaluate the thermodynamic and binding parameters. The intrinsic fluorescence of BSA was quenched by Nico- tine,and this quenching procedure was via a static mechanism. The thermodynamic parameters( AG, AH and AS)showed that the force between Nicotine and BSA was mainly hydrogen bonds and van der Waals interactions. The Fluorescence spectra of BSA with Nicotine in the presence of AgNPs were recorded at 298 K, and it was found the presence of AgNPs decrease the Stern-Volmer quenching constants Ksv ( 1.92 × 106 L- mol^-1 to 0. 82 × 106 L ·mol -1 ) and the binding constants K, ( 3.76 × 104 L·mol-1 to 1.73 × 104 L · mol^-1 ). In order to investigate the mechanism of AgNPs weaken the interaction of Nicotine and BSA, UV spectroscopy, synchronous fluorescence, infrared spectroscopy (IR) and circular dichroism (CD) methods were further used to study the interaction between BSA and AgNPs. The UV spectroscopy showed that the interaction was taken place between the BSA and the AgNPs as BSA was ad- sorbed to the surface of AgNPs. Analysis of synchronous? uorescence, infrared spectroscopy and circular dichroism showed that the binding of AgNPs to BSA would cause an apparent change in the secondary structure of BSA. All above results might have relevant consequence that AgNPs can be used to treat the craving for tobacco.
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