Deciphering the binding patterns and conformation changes upon the bovine serum albumin–rosmarinic acid complex

作者: Xin Peng , Xiangchao Wang , Wei Qi , Renliang Huang , Rongxin Su

DOI: 10.1039/C5FO00597C

关键词:

摘要: Rosmarinic acid (RA) is an importantly and naturally occurring polyphenol from plants of the mint family with potent biological activities. Here, in vitro interaction RA bovine serum albumin (BSA) has been investigated using various biophysical approaches as well molecular modeling methods, to ascertain its binding mechanism conformational changes. The fluorescence results demonstrated that quenching BSA by was mainly result formation a ground state BSA-RA complex, had one high affinity site constant 4.18 × 10(4) mol L(-1) at 298 K. Analysis thermodynamic parameters revealed hydrophobic hydrogen bond interactions were dominant intermolecular force complex formation. primary (site I) identified marker competitive experiments. distance between tryptophan residue evaluated 3.12 nm based on Forster's theory non-radiation energy transfer. UV-vis absorption, synchronous fluorescence, three-dimensional 8-anilino-1-naphthalenesulfonic (ANS) circular dichroism (CD), Fourier transform infrared (FT-IR) spectra confirmed conformation structure altered presence RA. Moreover, nuclear magnetic spectroscopy showed aromatic groups took part reaction during complexation. In addition, picture atomic level examined docking dynamics studies. brief, can bind noncovalent bonds relatively stable way, these findings will be beneficial functional food research

参考文章(57)
Xiangrong Li, Gongke Wang, Dejun Chen, Yan Lu, Binding of ascorbic acid and α-tocopherol to bovine serum albumin: a comparative study Molecular BioSystems. ,vol. 10, pp. 326- 337 ,(2014) , 10.1039/C3MB70373H
Zhenxing Chi, Rutao Liu, Yue Teng, Xiaoyan Fang, Canzhu Gao, Binding of oxytetracycline to bovine serum albumin: spectroscopic and molecular modeling investigations. Journal of Agricultural and Food Chemistry. ,vol. 58, pp. 10262- 10269 ,(2010) , 10.1021/JF101417W
John C Chatham, John R Forder, Lactic acid and protein interactions: implications for the NMR visibility of lactate in biological systems Biochimica et Biophysica Acta. ,vol. 1426, pp. 177- 184 ,(1999) , 10.1016/S0304-4165(98)00154-8
Maidul Hossain, Asma Yasmeen Khan, Gopinatha Suresh Kumar, None, Interaction of the Anticancer Plant Alkaloid Sanguinarine with Bovine Serum Albumin PLoS ONE. ,vol. 6, pp. e18333- ,(2011) , 10.1371/JOURNAL.PONE.0018333
Yan Liu, Jingjing Lin, Mingmao Chen, Ling Song, Investigation on the interaction of the toxicant, gentian violet, with bovine hemoglobin Food and Chemical Toxicology. ,vol. 58, pp. 264- 272 ,(2013) , 10.1016/J.FCT.2013.04.048
William L. Jorgensen, Jayaraman Chandrasekhar, Jeffry D. Madura, Roger W. Impey, Michael L. Klein, Comparison of simple potential functions for simulating liquid water The Journal of Chemical Physics. ,vol. 79, pp. 926- 935 ,(1983) , 10.1063/1.445869
Xingjia Guo, Lei Zhang, Xiudan Sun, Xiaowei Han, Chuang Guo, Pingli Kang, Spectroscopic studies on the interaction between sodium ozagrel and bovine serum albumin Journal of Molecular Structure. ,vol. 928, pp. 114- 120 ,(2009) , 10.1016/J.MOLSTRUC.2009.03.023
Bahram Hemmateenejad, Mojtaba Shamsipur, Fayezeh Samari, Taghi Khayamian, Malihe Ebrahimi, Zahra Rezaei, Combined fluorescence spectroscopy and molecular modeling studies on the interaction between harmalol and human serum albumin Journal of Pharmaceutical and Biomedical Analysis. ,vol. 67, pp. 201- 208 ,(2012) , 10.1016/J.JPBA.2012.04.012
Ying Yang, Xianyong Yu, Wenhua Tong, Shiyu Lu, Heting Liu, Qin Yao, Hu Zhou, Investigation of the Interaction Between Novel Spiro Thiazolo[3,2-a][1,3,5]Triazines and Bovine Serum Albumin by Spectroscopic Methods Journal of Solution Chemistry. ,vol. 42, pp. 666- 675 ,(2013) , 10.1007/S10953-013-9975-Z