INVESTIGATION ON THE INTERACTION OF β-SITOSTEROL AND LUTEOLIN-7-GLUCOSIDE BINDING TO BOVINE SERUM ALBUMIN
Keywords:β-sitosterol, Luteolin–7-glucoside, Bovine serum albumin, Molecular docking
Objective: The study ondrug–protein interactions is an important field of interest because of the prospective of unraveling of drug action mechanisms and the possibility of designing novel medicines. Bovine serum albumin (BSA) has been studied extensively because of its structural homology with human serum albumin (HSA). The objective of the work was to study the interaction between β-sitosterol and Luteolin–7-glucoside with bovine serum albumin (BSA) investigated by molecular docking.
Methods: Docking studies were carried out using a crystal structure of bovine serum albumin complexed with naproxen (pdb code-4OR0). Auto dock 4.2 was used to perform molecular docking. Ligands were found flexible during the docking process, and protein was kept rigid.
Results: Molecular docking studies revealed that the β-sitosterol can bind in the large hydrophobic cavity of BSA, mainly by the hydrophobic interaction but also by hydrogen bond interactions between the hydroxyl (OH) group of β-sitosterol to SER 488 with hydrogen bond distance of 2.1Å. Luteolin-7-glucoside molecule interact by hydrophobic interaction with LYS 431, ARG 427, ALA 193 amino acids of Bovine Serum Albumin. The amino acids ARG 458, ARG 435, ARG 185 are involved in forming a hydrogen bond with hydroxyl oxygens, carbonyl carbon of Luteolin-7-glucoside with hydrogen bond distance of 2.4, 2.3 and 1.9 Å, respectively.
Conclusion: Study indicated that hydrophobic and hydrogen bonding interactions were mostly responsible for albumin interaction. Further research of the pharmaceutical potential of plant molecules will be valuable for monitoring their biological functions.
Mutai C, Bii C, Vagias C, Abatis D, Roussis V. Antimicrobial activity of Acacia mellifera extracts and lupane triterpenes. J Ethnopharmacol. 2009;123(1):143-8. doi: 10.1016/j.jep.2009.02.007, PMID 19429353.
Cicero AFG, Fiorito A, Panourgia MP, Sangiorgi Z, Gaddi A. Effects of a new soy/β-sitosterol supplement on plasma lipids in moderately hypercholesterolemic subjects. J Am Diet Assoc. 2002;102(12):1807-11. doi: 10.1016/s0002-8223(02)90388-3, PMID 12487546.
Vivancos M, Moreno JJ. Effect of resveratrol, tyrosol and beta-sitosterol on oxidised low-density lipoprotein-stimulated oxidative stress, arachidonic acid release and prostaglandin E2 synthesis by RAW 264.7 macrophages. Br J Nutr. 2008;99(6):1199-207. doi: 10.1017/S0007114507876203, PMID 18081942.
Choi S, Kim KW, Choi JS, Han ST, Park YI, Lee SK. Angiogenic activity of beta-sitosterol in the ischaemia/reperfusion-damaged brain of Mongolian gerbil. Planta Med. 2002;68(4):330-5. doi: 10.1055/s-2002-26750, PMID 11988857.
Liu EH, Qi LW, Li P. Structural relationship and binding mechanisms of five flavonoids with bovine serum albumin. Molecules. 2010;15(12):9092-103. doi: 10.3390/molecules15129092, PMID 21150826.
Anbazhagan V, Renganathan R. Study on the binding of 2,3-diazabicyclo[2.2.2]oct-2-ene with bovine serum albumin by fluorescence spectroscopy. J Lumin. 2008;128(9):1454-8. doi: 10.1016/j.jlumin.2008.02.004.
Moriyama Y, Ohta D, Hachiya K, Mitsui Y, Takeda K. Fluorescence behavior of tryptophan residues of bovine and human serum albumins in ionic surfactant solutions: a comparative study of the two and one tryptophan(s) of bovine and human albumins. J Protein Chem. 1996;15(3):265-72. doi: 10.1007/BF01887115, PMID 8804574.
Garg S, Raghav N. Synthesis of novel chalcones of Schiff’s bases and to study their effect on bovine serum albumin. Asian J Pharm Clin Res. 2013;6(4):181-4.
PV, MS, BS. In vitro anti-arthritic activity of Cissus quadrangularis stem extract. Asian J Pharm Clin Res. 2019;12(1):250-2. doi: 10.22159/ajpcr.2019.v12i1.27353.
Waluyo DA, Sutriyo. Evaluation of anti-glycation effect and safety of serum anti-aging formulation containing gold nanoparticles (aunp) using sidaguri extract (Sida rhombifolia). Int J Appl Pharm. 2022;14(1):226-30. doi: 10.22159/ijap.2022v14i1.40417.
Ravikumar R, Verma Sc, Pal S, Maddi R, Murali Krishna C, Singh R. Evaluation of in vitro anti-inflammatory activity and HPTLC analysis of plant phyllanthus fraternus. Sarkar Bk. Int J Curr Pharm Res. 2017;9(5):198-200.
Lin CZ, Hu M, Wu AZ, Zhu CC. Investigation on the differences of four flavonoids with similar structure binding to human serum albumin. J Pharm Anal. 2014;4(6):392-8. doi: 10.1016/j.jpha.2014.04.001, PMID 29403905.
Sobhy R, Khalifa I, Liang H, Li B. Phytosterols disaggregate bovine serum albumin under the glycation conditions through interacting with its glycation sites and altering its secondary structure elements. Bioorg Chem. 2020;101:104047. doi: 10.1016/j.bioorg.2020.104047, PMID 32629289.
RCSB Protein Data Bank. Structure summary. RCSB PDB-4OR0: Crystal Structure of Bovine Serum Albumin in complex with naproxen structure; 2004. doi: 10.2210/pdb4OR0/pdb.
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