引用本文:
蔡雪梅, 李建晴, 卫艳丽, 董川. 分子内电荷转移荧光探针1-酮-2-(对二甲氨基苯亚甲基)-四氢萘与人血清白蛋白作用[J]. 应用化学,
2010, 27(11): 1313-1317.
doi:
10.3724/SP.J.1095.2010.00013
Citation: CAI Xue-Mei, LI Jian-Qing, WEI Yan-Li, DONG Chuan. Interactions Between an Intramolecular Charge Transfer Fluorescence Probe 1-Keto-2-(p-dimethylaminobenzal)-tetrohydronaphthalene and Human Serum Albumin[J]. Chinese Journal of Applied Chemistry, 2010, 27(11): 1313-1317. doi: 10.3724/SP.J.1095.2010.00013
Citation: CAI Xue-Mei, LI Jian-Qing, WEI Yan-Li, DONG Chuan. Interactions Between an Intramolecular Charge Transfer Fluorescence Probe 1-Keto-2-(p-dimethylaminobenzal)-tetrohydronaphthalene and Human Serum Albumin[J]. Chinese Journal of Applied Chemistry, 2010, 27(11): 1313-1317. doi: 10.3724/SP.J.1095.2010.00013
分子内电荷转移荧光探针1-酮-2-(对二甲氨基苯亚甲基)-四氢萘与人血清白蛋白作用
摘要:
采用荧光及紫外光谱研究了1-酮-2-(对二甲氨基苯亚甲基)-四氢萘(KDTN)与人血清白蛋白(HSA)相互作用的光谱特性。结果表明,静态猝灭和非辐射能量转移是导致KDTN对HSA荧光猝灭的主要原因。测得17、27和37℃3个温度下的结合常数KA分别为1.633×108、0.7998×108和0.347×108L/mol,结合位点数n分别为1.7、1.6和1.7;据Förster偶极-偶极非辐射能量转移理论,计算得到KDTN与HSA在3个温度下的作用距离r分别为2.64、2.59和2.64nm;能量转移效率E分别为0.5100、0.4797和0.4210。热力学参数表明,二者主要以范德华力或氢键结合;用同步荧光技术研究了KDTN对HSA构象的影响,结果表明,KDTN的加入对HSA构象影响不大。
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关键词:
- 酮-(对二甲氨基苯亚甲基)-四氢萘
- / 人血清白蛋白
- / 荧光光谱法
English
Interactions Between an Intramolecular Charge Transfer Fluorescence Probe 1-Keto-2-(p-dimethylaminobenzal)-tetrohydronaphthalene and Human Serum Albumin
Abstract:
The interactions between 1-Keto-2-(p-dimethylaminobenzal)-tetrohydronaphthalene(KDTN) and human serum albumin(HSA) have been studied by fluorescence and UV-Vis absorption spectra.The binding of KDTN to HSA quenches the tryptophan residue fluorescence and the results show that static quenching occurrs together with the complex formation.The binding constant and binding sites of KDTN to HSA at pH=7.43 are measured at different temperatures according to the double logarithm regression curve.In addition,the thermodynamic data show that KDTN molecules enter the hydrophobic cavity of HSA via Van der Waals force or hydrogen bond.Finally,the synchronous fluorescence spectra show that the microenvironment of the tryptophan residues does not show significant effect on the conformation.
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