1.西华大学理学院,四川 成都 610039
2.兰州大学化学化工学院,甘肃 兰州 730000
王会镇(1988年生),男;研究方向:有机合成化学;E-mail:578527840@qq.com
刘家琴(1967年生),女;研究方向:分析化学;E-mail:liujq2015@126.com
纸质出版日期:2021-11-25,
网络出版日期:2021-04-23,
收稿日期:2020-06-25,
录用日期:2020-08-21
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王会镇,雷琴,张弛翔等.3-[2-(5-溴-噻吩基)]-1-苯基-2-丙烯酮与牛血清白蛋白的相互作用[J].中山大学学报(自然科学版),2021,60(06):121-127.
WANG Huizhen,LEI Qin,ZHANG Chixiang,et al.The interaction of 3-[2-(5-Bromo-thienyl)]-1-phenyl-2-propenone with bovine serum albumin[J].Acta Scientiarum Naturalium Universitatis Sunyatseni,2021,60(06):121-127.
王会镇,雷琴,张弛翔等.3-[2-(5-溴-噻吩基)]-1-苯基-2-丙烯酮与牛血清白蛋白的相互作用[J].中山大学学报(自然科学版),2021,60(06):121-127. DOI: 10.13471/j.cnki.acta.snus.2020C014.
WANG Huizhen,LEI Qin,ZHANG Chixiang,et al.The interaction of 3-[2-(5-Bromo-thienyl)]-1-phenyl-2-propenone with bovine serum albumin[J].Acta Scientiarum Naturalium Universitatis Sunyatseni,2021,60(06):121-127. DOI: 10.13471/j.cnki.acta.snus.2020C014.
通过苯乙酮和5-溴噻吩-2-甲醛合成了3-[2-(5-溴-噻吩基)]-1-苯基-2-丙烯酮 (BTPPO)。使用光谱法和分子对接模拟研究了BTPPO与牛血清白蛋白(BSA,bovine serum albumin)的作用过程。同时,研究了金属离子 (Cu
2+
Co
2+
Pb
2+
Ag
+
Hg
2+
Cd
2+
) 对BTPPO与BSA相互作用的影响。结果表明:BTPPO与BSA的作用主要是静态荧光淬灭过程,两者之间的结合以疏水和静电作用为主,结合常数 (
K
a
) 为10
4
左右。根据Förster理论,可以计算得BTPPO和BSA的共振能量转移距离小于7 nm。另外,在280 nm和295 nm激发波长下蛋白质的荧光淬灭实验表明:BTPPO与BSA的主要结合位点是BSA的亚结构域ⅡA (siteⅠ)。金属离子(Pb
2+
除外)的存在可能会影响BTPPO荧光淬灭效果。分子对接模拟结果表明:BTPPO是通过疏水和极性作用嵌入BSA分子的亚结构域ⅡA (siteⅠ) 的疏水腔内的。
3-[2-(5-Bromo-thienyl)]-1-phenyl-2-propenone (BTPPO) was synthesized from acetophenone and 5-bromothiophene-2-carbaldehyde. The spectrometric and molecular docking were employed to investigate the binding mechanism of BTPPO to bovine serum albumin (BSA)
and the effects of metal ions (Cu
2+
Co
2+
Pb
2+
Ag
+
Hg
2+
Cd
2+
) on the BTPPO-BSA binding system were also discussed. The spectrometric experiment results showed that the binding reaction of BTPPO to BSA was based on the static fluorescence-quenching process with hydrophobic and electrostatic forces
and the binding constant (
K
a
) was about 10
4
. Based on the Förster theory
the binding distance (
r
) between BTPPO and BSA was less than 7 nm. Comparing the quenching of protein fluorescence excited at 280 nm and 295 nm
it was shown that the primary BTPPO binding site was located in the sub-domain ⅡA (siteⅠ) of BSA. The presence of metal ions (except Pb
2+
) may influence the BTPPO efficacy. The molecule docking results illustrated that BTPPO can bind with the sub-domain ⅡA of BSA in which hydrophobic and polar interactions are the key acting force.
3-[2-(5-溴-噻吩基)]-1-苯基-2-丙烯酮 (BTPPO)牛血清白蛋白(BSA,bovine serum albumin)结合机理荧光分子对接
3-[2-(5-Bromo-thienyl)]-1-phenyl-2-propenone (BTPPO)bovine serum albumin(BSA)binding mechanismfluorescencemolecule docking
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