化学研究与应用
化學研究與應用
화학연구여응용
CHEMICAL RESEARCH AND APPLICATION
2013年
8期
1073-1077
,共5页
盐酸胺碘酮%碳纳米管%牛血清白蛋白%荧光光谱%相互作用
鹽痠胺碘酮%碳納米管%牛血清白蛋白%熒光光譜%相互作用
염산알전동%탄납미관%우혈청백단백%형광광보%상호작용
amiodarone hydrochloride(AD)%carbon nanotubes(CNTs)%bovine serum albumin(BSA)%fluorescence spectroscopy%interaction
在pH 7.40的Tris-HCl缓冲体系下，用荧光光谱法研究了碳纳米管（ MCNTs）对盐酸胺碘酮（ AD）和牛血清白蛋白（ BSA）荧光光谱特性的影响以及无碳纳米管共存时盐酸胺碘酮与BSA之间的相互作用。结果表明，AD对BSA的荧光有较强的猝灭作用，其猝灭机理为动态猝灭。碳纳米管的存在使AD对BSA的猝灭作用增强。计算了不同温度下AD与BSA之间的表观结合常数KA ，结合位点数n。相应的热力学参数ΔH、ΔG和ΔS表明，AD与BSA之间主要以静电作用力结合。根据F?rster非辐射能量转移理论，确定了AD与BSA之间的结合距离r＝3.99 nm。此外，利用同步荧光光谱，分析了AD对BSA构象的影响。在碳纳米管存在下， AD与BSA结合位点数增加，其结合常数也高于无MCNTs时的KA值，MCNTs的加入没有引起BSA构象的变化。
在pH 7.40的Tris-HCl緩遲體繫下，用熒光光譜法研究瞭碳納米管（ MCNTs）對鹽痠胺碘酮（ AD）和牛血清白蛋白（ BSA）熒光光譜特性的影響以及無碳納米管共存時鹽痠胺碘酮與BSA之間的相互作用。結果錶明，AD對BSA的熒光有較彊的猝滅作用，其猝滅機理為動態猝滅。碳納米管的存在使AD對BSA的猝滅作用增彊。計算瞭不同溫度下AD與BSA之間的錶觀結閤常數KA ，結閤位點數n。相應的熱力學參數ΔH、ΔG和ΔS錶明，AD與BSA之間主要以靜電作用力結閤。根據F?rster非輻射能量轉移理論，確定瞭AD與BSA之間的結閤距離r＝3.99 nm。此外，利用同步熒光光譜，分析瞭AD對BSA構象的影響。在碳納米管存在下， AD與BSA結閤位點數增加，其結閤常數也高于無MCNTs時的KA值，MCNTs的加入沒有引起BSA構象的變化。
재pH 7.40적Tris-HCl완충체계하，용형광광보법연구료탄납미관（ MCNTs）대염산알전동（ AD）화우혈청백단백（ BSA）형광광보특성적영향이급무탄납미관공존시염산알전동여BSA지간적상호작용。결과표명，AD대BSA적형광유교강적졸멸작용，기졸멸궤리위동태졸멸。탄납미관적존재사AD대BSA적졸멸작용증강。계산료불동온도하AD여BSA지간적표관결합상수KA ，결합위점수n。상응적열역학삼수ΔH、ΔG화ΔS표명，AD여BSA지간주요이정전작용력결합。근거F?rster비복사능량전이이론，학정료AD여BSA지간적결합거리r＝3.99 nm。차외，이용동보형광광보，분석료AD대BSA구상적영향。재탄납미관존재하， AD여BSA결합위점수증가，기결합상수야고우무MCNTs시적KA치，MCNTs적가입몰유인기BSA구상적변화。
Under the pH 7.40 Tris-HCl buffer system , fluorescence spectroscopy was used to investigate the influences of carbon nanotubes(CNTs)on the fluorescence of amiodarone hydrochloride (AD)on bovine serum albumin(BSA)and the influences of AD on that of BSA without CNTs.The experimental results demonstrated that AD could quench the intrinsic fluorescence of BSA ,and the quenching mechanism was dynamic quenching.The fluorescence quenching action of AD on BSA was strengthened in the pres-ence of CNTs.The binding constants KA,binding sites n and the corresponding thermodynamic parameters ΔH,ΔG andΔS at differ-ent temperatures were calculated.Based on the thermodynamic parameters ,it was proved that the major roles of binding force of AD-BSA was the electrostatic.The distance r of AD-BSA was evaluated according to the theory of F?ster energy transfer.Moreover,the effect of AD on the conformation of BSA was also analyzed by using synchronous fluorescence spectroscopy .The results showed that AD changed the conformation of BSA during the reaction.But the CNTs could not change the conformation of BSA.The binding con-stants KA ,binding sites n of AD on BSA was increased in the presence of CNTs .The discussion offer a reference study on the action mechanism of CNTs and AD with albumin in vivo .
