Molecular insight into binding behavior of polyphenol (rutin) with beta lactoglobulin: Spectroscopic, molecular docking and MD simulation studies

被引:129
|
作者
Al-Shabib, Nasser Abdulatif [1 ]
Khan, Javed Masood [1 ]
Malik, Ajamaluddin [2 ]
Alsenaidy, Mohammad A. [3 ]
Rehman, Md Tabish [4 ]
AlAjmi, Mohamed F. [4 ]
Alsenaidy, Abdulrahman M. [2 ]
Husain, Fohad Mabood [1 ]
Khan, Rizwan Hasan [5 ]
机构
[1] King Saud Univ, Fac Food & Agr Sci, Dept Food Sci & Nutr, Riyadh 11451, Saudi Arabia
[2] King Saud Univ, Coll Sci, Dept Biochem, Prot Res Chair, Riyadh, Saudi Arabia
[3] King Saud Univ, Coll Pharm, Dept Pharmaceut, Riyadh, Saudi Arabia
[4] King Saud Univ, Coll Pharm, Dept Pharmacognosy, Riyadh 11451, Saudi Arabia
[5] Aligarh Muslim Univ, Interdisciplinary Biotechnol Unit, Mol Biophys & Biophys Chem Grp, Aligarh 202002, Uttar Pradesh, India
关键词
Rutin; Flavonoid; Protein-ligand interaction; beta lactoglobulin; CD; Molecular docking; HUMAN SERUM-ALBUMIN; BOVINE; FLAVONOIDS; DRUG; JATRORRHIZINE; LIPOCALIN;
D O I
10.1016/j.molliq.2018.07.122
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The interaction of natural polyphenolic compounds (rutin) with beta-lactoglobulin (BLG) was carried out by using several optical spectroscopic (UV-visible spectroscopy, fluorescence quenching measurements, synchronous fluorescence, 3D fluorescence spectroscopy and far-UV CD measurements), molecular docking and molecular dynamics (MD) simulation methods. The fluorescence quenching results confirmed that fluorescence intensity of BLG is quenched by rutin and the quenching constant is increased with increase in temperature. The quenching mechanism between rutin-BLG was found to be dynamic in nature. The thermodynamic parameter particularly Delta H-0 and Delta S-0 obtained through fluorescence measurements clearly indicated that hydrophobic forces are majorly involved in the rutin-BLG interaction. The UV-absorption, synchronous and three-dimensional fluorescence results displayed that the micro-environment of BLG is changed due to rutin interaction. The secondary structure of BLG was found higher in the presence of rutin. Molecular docking results suggested that rutin binds strongly in the internal cavity of BLG at site 1 and superficially at site 2 through both hydrogen bonding and hydrophobic interactions. The binding affinity was found to be higher 5.47 x 10(6) M-1 for site 1 compared to site 2 (2.86 x 10(5) M-1). The MD simulation suggested that rutin formed a stable complex with BLG at site].This study will explain interacting properties of rutin with carrier BLG proteins and open a new vista for the food industry. (C) 2018 Elsevier B.V. All rights reserved.
引用
收藏
页码:511 / 520
页数:10
相关论文
共 50 条
  • [1] The Interaction of Polyphenol Flavonoids with β-lactoglobulin: Molecular Docking and Molecular Dynamics Simulation Studies
    Sahihi, Mehdi
    Heidari-Koholi, Zobeideh
    Bordbar, Abdol-Khalgh
    JOURNAL OF MACROMOLECULAR SCIENCE PART B-PHYSICS, 2012, 51 (12): : 2311 - 2323
  • [2] Molecular insight into binding behavior of caffeine with lactoferrin: Spectroscopic, molecular docking, and simulation study
    Li, Zekun
    Li, Zhixi
    Ma, Haorui
    Fu, Shangchen
    Liu, Guanxu
    Hao, Changchun
    Liu, Yongfeng
    JOURNAL OF DAIRY SCIENCE, 2023, 106 (12) : 8249 - 8261
  • [3] Binding of biguanides to β-lactoglobulin: molecular-docking and molecular dynamics simulation studies
    Mehdi Sahihi
    Yousef Ghayeb
    Chemical Papers, 2014, 68 : 1601 - 1607
  • [4] Binding of biguanides to β-lactoglobulin: molecular-docking and molecular dynamics simulation studies
    Sahihi, Mehdi
    Ghayeb, Yousef
    CHEMICAL PAPERS, 2014, 68 (11) : 1601 - 1607
  • [5] Spectroscopic, molecular docking and molecular dynamic simulation studies on the complexes of β-lactoglobulin, safranal and oleuropein
    Vanaei, Shohreh
    Parizi, Mohammad Salemizadeh
    Abdolhosseini, Saeed
    Katouzian, Iman
    INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2020, 165 : 2326 - 2337
  • [6] Interaction of β-Lactoglobulin with Resveratrol: Molecular Docking and Molecular Dynamics Simulation Studies
    Sahihi, M.
    Ghayeb, Y.
    Bordbar, A. Khalegh
    CHEMICAL AND BIOCHEMICAL ENGINEERING QUARTERLY, 2013, 27 (04) : 417 - 422
  • [7] Study on simultaneous binding of resveratrol and curcumin to β-lactoglobulin: Multi-spectroscopic, molecular docking and molecular dynamics simulation approaches
    Zhang, Xiaoge
    Lu, Yingcong
    Zhao, Ru
    Wang, Ce
    Wang, Cuina
    Zhang, Tiehua
    FOOD HYDROCOLLOIDS, 2022, 124
  • [8] Structural stability of β-lactoglobulin in the presence of cetylpyridinum bromide: spectroscopic and molecular docking studies
    Chavoshpour-Natanzi, Zahra
    Sahihi, Mehdi
    Gharaghani, Sajjad
    JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 2018, 36 (03): : 753 - 760
  • [9] Simultaneous binding of folic acid and lutein to ?-lactoglobulin and ?-lactalbumin: A spectroscopic and molecular docking study
    Vidotto, Danilo C.
    Tavares, Guilherme M.
    FOOD BIOSCIENCE, 2022, 50
  • [10] Spectroscopic, Thermodynamic and Molecular Docking Studies on Molecular Mechanisms of Drug Binding to Proteins
    Wani, Tanveer A.
    Zargar, Seema
    Hussain, Afzal
    MOLECULES, 2022, 27 (23):