Investigation of Triamcinolone-Bovine Serum Albumin (BSA) Interaction by Spectroscopic Methods

Year 2020, Volume: 7 Issue: 3, 903 - 910, 30.10.2020

Sabriye Aydınoğlu

https://doi.org/10.18596/jotcsa.782263

Abstract

The aim of the present study was investigate the interaction between bovine serum albumin and triamcinolone. For this purpose, the interaction between BSA and triamcinolone was evaluated by UV–Vis and fluorescence spectroscopy under different temperatures, and different salt concentration at physiological pH (7.4). The binding constant of BSA-Triamcinolone system were evaluated different temperature at constant (pH =7.4) and ionic strength (0.01 M). The binding constant dependence of binding constant on temperature was analysed by Van’t Hoff equation. The standard enthalpy change (DeltaH) and standard entropy change (DeltaS) values were determinated respectively as 9.0 kcal/mol while as 54.1 cal/mol.K.. In addition, the effect of salt concentration investigated for BSA-Triamcinolone system at constant temperature (T=25°C) and increasing salt concentration lead to decrement on the binding constant value. The obtained thermodynamic parameters indicate hydrophobic forces take major role in BSA-Triamcinolone interaction. The arousal of salt concentration prompted to diminution on affinity between Triamcinolone and BSA.

Keywords

Triamcinolone, Bovine Serul Albumin, Drug Protein Interaction, Thermodynamics, Spectroscopy

References

• Fasano M, Curry S, Terreno E, Galliano M, Fanali G, Narciiso P, Notari S, Ascenzi P. The extraordinary ligand binding properties of human serum albumin. IUBMB, Life. 2005; 57: 787 – 96. Doi: 10.1080/15216540500404093.
• Rizzuti B, Bartucci R, Pey AL, Guzzi R. Warfarin increases thermal resistance of albumin through stabilization of the protein lobe that includes its binding site. Archives of Biochemistry and Biophysics. 2019; 676:(108123) 1-8. Doi: 10.1016/j.abb.2019.108123.
• Pilati D, Kenneth A. Howard Albumin-based drug designs for pharmacokinetic modulation. Expert Opinion on Drug Metabolism & Toxicology. 2020; Doi: 10.1080/17425255.2020.1801633.
• Wilting J, Van Der Giesen WF, Janssen LHM. The effect of chloride on the binding of warfarin to albumin as a function of pH. Biochemical Pharmacology. 1981:1025-31. Doi:10.1016/j.proeng.2010.09.152.
• Kandagal PB, Ashoka S, Seetharamappa J, Shaikh SMT, Jadegoud Y, Ijare OB. Study of the interaction of an anticancer drug with human and bovine serum albumin spectroscopic approach. Journal of Pharmaceutical and Biomedical Analysis. 2006; 41: 393–9. Doi: 10.1016/j.jpba.2005.11.037.
• Fender AC, Dobrev D. Bound to bleed: How altered albumin binding may dictate warfarin treatment outcome. IJC Heart & Vasculature. 2019; 22: 214-5.
• Al-Harthi S, Lachowicz JI, Nowakowski ME. Towards the functional high-resolution coordination chemistry of blood plasma human serum albumin. Journal of Inorganic Biochemistry. 2019; 198: (110716) 1-15.
• Seedher N, Bhatia S. Mechanism of interaction of the non-steroidal antiinflammatory drugs meloxicam and nimesulide with serum albumin. Journal of Pharmaceutical and Biomedical Analysis. 2005; 39: 257-69.
• Sharifi M, Dolatabadi JEN, Fathi F, Rashidi M, JafariB, Tajalli H, Rashidi MR. Kinetic and thermodynamic study of bovine serum albumin interaction with rifampicin using surface plasmon resonance and molecular docking methods. Journal of Biomedical Optics. 2017; 22: (037002)1-6. Doi: 10.1117/1.JBO.22.3.037002.
• Raghav D, Mahanty S, Rathinasamy K. Characterizing the interactions of the antipsychotic drug trifluoperazine with bovine serum albumin: Probing the drug-protein and drug-drug interactions using multi-spectroscopic approaches. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 2020; 226: (117584) 1-14. doi: 10.1016/j.saa.2019.117584.
• Chakraborty B, Basu S. Interaction of BSA with proflavin: A spectroscopic approach. Journal of Luminescence. 2009; 129: 34-9. Doi: 10.1016/j.jlumin.2008.07.012.
• Jha NS, Kishore N. Thermodynamic studies on the interaction of folic acid with bovine serum albumin. The Journal of Chemical Thermodynamics. 2011; 43: 814-21. Doi: 10.1016/j.jct.2010.12.024.
• Tian J, Liu J, Hu Z, Chen X. Interaction of wogonin with bovine serum albumin. Bioorganic & Medicinal Chemistry. 2005; 13: 4124–9. Doi: 10.1016/j.bmc.2005.02.065.
• Goyal RN, Gupta VK, Chatterjee S. A sensitive voltammetric sensor for determination of synthetic corticosteroid triamcinolone abused for doping. Biosensors and Bioelectronics. 2009; 3562-8. Doi: 10.1016/j.bios.2009.05.016.
• Chaires JB. Energetics of Drug–DNA. Current Opinion in Structural Biology. 1998; 8:314-20.
• Macii F, Salvadori G, Bonini R, Giannarelli S, Mennucci B, Biver T. Binding of model polycyclic aromatic hydrocarbons andcarbamate-pesticides to DNA, BSA, micelles and liposomes. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 2019; 223: (117313)1-9. Doi: 10.1016/j.saa.2019.117313.
• Aydinoglu S, Biver T, Figuccia S, Fiore T, Montanaro S, Pellerito C. Studies on DNA interaction of organotin(IV) complexes of meso-tetra(4-sulfonatophenyl)porphine that show cellular activity. Journal of Inorganic Biochemistry. 2016; 163: 311–7. Doi: 10.1016/j.jinorgbio.2016.06.030
• Beccia MR, Biver T, Pardini A, Spinelli J, Secco F, Venturini M, , Jacopo Spinelli, Fernando Secco, Marcella Venturini, Vázquez Busto N, Cornejo Lopez MP, Martin Herrera VI, Gotor RP. The fluorophore 4',6-diamidino-2-phenylindole (DAPI) induces DNA folding in long double-stranded DNA. Chemistry - An Asian Journal. 2012; 7; 1803-10. Doi: 10.1002/asia.201200177.