Abstract：The interaction between 20(S)-protopanaxatriol (PPT) and bovine serum albumin ( BSA) was studied with fluorescence quenching technique and ultra-violet absorption spectroscopy. The results indicated that PPT led to the intrinsic fluorescence quenching of BSA through a static quenching process .The binding constants of PPT with BSA obtained with fluorescence quenching method were calculated as 0.926 3×103 (298 K), 0.618 2×103 (308 K), 0.414 4×103 L·mol-1(318 K), respectively; while the number binding sites n were close to unity. The results showed that the driving force of the interaction between PPT and BSA was hydrogen bond and Van der Waals force. The result of synchronous fluorescence spectra showed that binding of PPT with BSA could induce conformational changes in BSA, that the part of tryptophan became more closely. According to Fster fluorescence resonance energy transfer theory, the binding distance r and energy-transfer efficiency E were respectively 26.2 nm and 0.32.
张钊华，迟绍明，盘振杰，李志文，李亚娟，胡天凤，陈艳梅，赵 焱* . 荧光光谱法研究20(S)-原人参三醇与牛血清白蛋白的相互作用 [J]. 光谱学与光谱分析, 2016, 36(12): 3991-3995.
ZHANG Zhao-hua, CHI Shao-ming, PAN Zhen-jie, LI Zhi-wen, LI Ya-juan, HU Tian-feng, CHEN Yan-mei, ZHAO Yan* . Fluorescence Spectroscopic Studies on Binding of 20(S)-Protopanaxatriol with Bovine Serum Albumin . SPECTROSCOPY AND SPECTRAL ANALYSIS, 2016, 36(12): 3991-3995.
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