The interaction of 3-［2-（5-Bromo-thienyl）］-1-phenyl-2-propenone with bovine serum albumin

WANG Huizhen; LEI Qin; ZHANG Chixiang; YAO Xiaojun; CHEN Shaoling; LIU Jiaqin; WANG Yan

doi:10.13471/j.cnki.acta.snus.2020C014

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The interaction of 3-［2-（5-Bromo-thienyl）］-1-phenyl-2-propenone with bovine serum albumin

Research articles | 更新时间：2023-11-01

- The interaction of 3-［2-（5-Bromo-thienyl）］-1-phenyl-2-propenone with bovine serum albumin
- Acta Scientiarum Naturalium Universitatis Sunyatseni Vol. 60, Issue 6, Pages: 121-127(2021)
- 作者机构：
  
  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
- 作者简介：
- 基金信息：
- DOI：10.13471/j.cnki.acta.snus.2020C014
  CLC： O657.3
- Published：25 November 2021，
  
  Published Online：23 April 2021，
  
  Received：25 June 2020，
  
  Accepted：21 August 2020
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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.

摘要

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

) 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 (

) 为10

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

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。

Abstract

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

) 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 (

) was about 10

. Based on the Förster theory

the binding distance (

) 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

) 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.

关键词

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

Keywords

3-[2-(5-Bromo-thienyl)]-1-phenyl-2-propenone （BTPPO）bovine serum albumin（BSA）binding mechanismfluorescencemolecule docking

references

KRATZ F. Albumin as a drug carrier： Design of prodrugs drug conjugates and nanoparticles［J］. J Controlled Release， 2008， 132： 171-183.

ABASSI P， ABASSI F， YARI F， et al. Study on the interaction of sulforaphane with human and bovine serum albumins［J］. Journal of Photochemistry and Photobiology B： Biology， 2013， 122： 61-67.

TIAN Z Y， ZANG F L， LUO W， et al. Spectroscopic study on the interaction between mononaphthalimide spermidine （MINS） and bovine serum albumin （BSA）［J］. Journal of Photochemistry and Photobiology B： Biology， 2015， 142： 103-109.

EMIT M D， BYADAGI K S， NANDIBEWOOR S T， et al. Multi-spectral characterization & effect of metal ions on the binding of bovine serum albumin upon interaction with a lincosamide antibiotic drug［J］. Journal of Photochemistry and Photobiology B： Biology， 2014，138： 324-330.

CARTER D C， HO J X. Structure of serum albumin［J］. Advances in Protein Chemistry， 1994， 45： 153-203.

NOWAKOWSKA Z. A review of anti-infective and anti-inflammatory chalcones［J］. European Journal of Medicinal Chemistry， 2007， 42： 125-137.

DUCKI S. A review of anti-infective and anti-inflammatory chalcones［J］. Anti-Cancer Agents in Medicinal Chemistry， 2009， 9： 336-347.

LAKOWICZ J R. Principles of fluorescence spectroscopy［M］. New York： Kluwer Academic/Plenum Publishers， 1999.

LIGPREP， version 2.3， Schrödinger， LLC［CP］. New York， 2009.

KAMINSKI G A， FRIESNER R A， JORGENSEN W L， et al. Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides［J］.Journal of Physical Chemistry B， 2001， 105： 6474-6487.

EPIK， version 2.0， Schrödinger， LLC［CP］. New York， 2009.

BUJACZ A， ZIELINSKI K， SEKULA B. Structural studies of bovine， equine， and leporine serum albumin complexes with naproxen［J］.Proteins， 2014， 82： 2199-2208.

GLIDE， version 5.5， Schrödinger， LLC［CP］. New York， 2009.

ZHANG Y N， YANG L L， ZHOU P， et al. Fluorescent emission of coumaric aldehyde molecule enhanced by dihydrogen phosphate［J］. Chinese Journal of Luminescence， 2011， 32（9）： 962-967.

SHU Y， XUE W W， XU X Y， et al. Interaction of erucic acid with bovine serum albumin using a multi-spectroscopic method and molecular docking technique［J］. Food Chemistry， 2015， 173： 31-37.

LI X R， CHEN D J， WANG G K， et al. Study of interaction between human serum albumin and three antioxidants： Ascorbic acid， α-tocopherol， and proanthocyanidins ［J］. European Journal of Medicinal Chemistry， 2013， 70： 22-36.

BI S Y， PANG B， WANG T J， et al. Investigation on the interactions of clenbuterol to bovine serum albumin and lysozyme by molecular fluorescence technique［J］.Spectrochimica Acta Part A： Molecular and Biomolecular Spectroscopy， 2014， 120： 456-461.

EFTINK M R， GHIRON C A. Fluorescence quenching of indole and model micelle systems ［J］. The Journal of Chemical Physics， 1976， 80： 486-493.

NEMÉTHY G， SCHERAGA H A. Structure of water and hydrophobic bonding in proteins. I. A model for the thermodynamic properties of liquid water［J］. The Journal of Chemical Physics， 1962， 66： 1773-1789.

TIMASHEFF S N. In proteins of biological fluids［M］.Oxford：Pergamon Press， 1972.

ROSS P D， SUBRAMANIAN S. Thermodynamics of protein association reactions： Forces contributing to stability biochemistry［J］.Biochemistry， 1981， 20： 3096-3102.

FÖRSTER T， SINANOGLU O. Modern quantum chemistry［M］. New York： Academic Press， 1965.

ZHANG G C， WANG Y Q， ZHANG H M， et al. Human serum albumin interaction with paraquat studied using spectroscopic methods［J］. Pesticide Biochemistry and Physiology， 2007， 87： 23-29.

DING F， PAN H， LI Z Y， et al. Spectroscopic studies on the binding of barbital to bovine serum albumin［J］. Journal of Luminescence， 2009， 129： 650-655.

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