Analysis of aceclofenac and bovine serum albumin interaction using fluorescence quenching method for predictive, preventive, and personalized medicine

EPMA Journal

Md. Zakir Sultan¹  Mohammad Shah Amran²  Shaila Kabir²  Sangita Paul Kundu²  Sabiha Ferdowsy Koly² 

[1] Centre for Advanced Research in Sciences, University of Dhaka, Dhaka-1000, Bangladesh;Department of Pharmaceutical Chemistry, Faculty of Pharmacy, University of Dhaka, Dhaka-1000, Bangladesh

关键词: Thermodynamic parameter;    Drug-protein binding;    Fluorescence spectroscopy;    Bovine serum albumin;    Aceclofenac;    Predictive, preventive, and personalized medicine;   

Others  :  1235136
DOI  :  10.1186/s13167-015-0047-x

 received in 2015-09-04, accepted in 2015-12-03,  发布年份 2015

【 摘 要 】

Background

The study of the interaction of a drug with plasma protein is very important because drug-protein binding plays an important role in determination of pharmacological and toxicological properties of drugs. Our study was designed to investigate the interaction between aceclofenac and bovine serum albumin (BSA) using fluorescence spectroscopy at different temperatures (298 and 308 K).

Methods

Fluorescence spectroscopy was used to carry out the study. Fluorescence quenching constant was determined from Stern-Volmer equation. Van’t Hoff equation was used to determine the thermodynamic parameters such as free energy (ΔG), enthalpy (ΔH), and entropy (ΔS).

Results

The experimental data showed that the quenching of BSA by aceclofenac was due to a formation of a BSA-aceclofenac complex with probable involvement of both tryptophan and tyrosine residues of BSA. Dynamic quenching was shown for BSA by aceclofenac at the experimental conditions. The values of thermodynamic parameters indicated that the hydrophobic forces played major roles for BSA-aceclofenac complexation. The binding number (n) was found to be ≈1 indicating that 1 mol of BSA bound with 1 mol of aceclofenac. The binding affinity of aceclofenac to BSA was calculated at different temperatures. It was shown that the binding constant decreased with increasing temperatures indicating that stability of the BSA-aceclofenac complex decreased with increasing temperatures.

Conclusions

The interaction of aceclofenac with BSA was successfully explored using a fluorescence spectroscopic technique.

【 授权许可】

   
2015 Koly et al.

【 图 表 】

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【 参考文献 】

• [1]Flarakos J, Morand K, Vouros P. High-throughput solution based medicinal library screening against human serum albumin. Anal Chem. 2005; 77:1345-53.
• [2]Mallick A, Bera SC, Maiti S, Chattopadhyay N. Fluorometric investigation of interaction of 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a] quinolizine with bovine serum albumin. Biophys Chem. 2004; 112:9-14.
• [3]Ni Y, Liu GL, Kokot S. Competitive binding of small molecules with biopolymers: a fluorescence spectroscopy and chemometrics study of the interaction of aspirin and ibuprofen with BSA. Analyst. 2011; 136:4794-801.
• [4]Gentili PL, Ortica F, Favaro G. Static and dynamic interaction of a naturally occurring photochromic with bovine serum albumin studied by UV-visible absorption and fluorescence spectroscopy. J Phys Chem B. 2008; 112:16793-801.
• [5]Kandagal PB, Ashoka S, Seetharamappa J, Shaikh SM, Jadegoud Y, Ijare OB. Study of the interaction of an anticancer drug with human and bovine serum albumin: spectroscopic approach. J Pharm Biomed Anal. 2006; 41(2):393-9.
• [6]He XM, Carter DC. Atomic structure and chemistry of human serum albumin. Nature. 1992; 358:209-15.
• [7]Hu YJ, Yi L, Zhang LX, Zhao RM, Qu SS. Studies of interaction between colchicine and bovine serum albumin by fluorescence quenching method. J Mol Struct. 2005; 750:174-8.
• [8]Wang YQ, Zhang HM, Zhang GC. Studies of the interaction between palmatine hydrochloride and human serum albumin by fluorescence quenching method. J Pharm Biomed Anal. 2006; 41:1041-6.
• [9]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 Luminesc. 2008; 128(9):1454-8.
• [10]Liu J, Tian J, Li Y, Yao X, Hu Z, Chen X. Binding of the bioactive component daphnetin to human serum albumin demonstrated using tryptophan fluorescence quenching. Macromol Biosci. 2004; 4(5):520-5.
• [11]Piniella JF, Larena A, Carrasco E, Ginebreda E, Julia S, Germain G. Crystal structure and spectroscopic study of 2-[2,6-dichlorophenyl)amino]phenylacetoxyacetic acid (aceclofenac). J Chem Crystallograp. 1992; 22:323-8.
• [12]Golubnitschaja O, Costigliola V. General report & recommendations in predictive, preventive and personalised medicine 2012: white paper of the European Association for Predictive, Preventive and Personalised Medicine. EPMA J. 2012; 3(1):14. BioMed Central Full Text
• [13]Steinhardt J, Krijn J, Leidy JG. Differences between bovine and human serum albumins: binding isotherms, optical rotatory dispersion, viscosity, hydrogen ion titration, and fluorescence effects. Biochemistry. 1971; 10:4005-15.
• [14]Bhattacharyya M, Chaudhuri U, Poddar RK. Evidence for cooperative binding of chlorpromazine with hemoglobin: equilibrium dialysis, fluorescence quenching and oxygen release study. Biochem Biophys Res Commun. 1990; 167:1146-53.
• [15]Rasoulzadeh F, Asgari D, Naseri A, Rashidi MR. Spectroscopic studies on the interaction between erlotinib hydrochloride and bovine serum albumin. Daru. 2010; 18:179-84.
• [16]Lakowicz JR. Principles of fluorescence spectroscopy. 2nd ed. Plenum Press, New York; 1999.
• [17]Kaushelendra M, Himesh S, Govind N, Sita SP, Singhai AK. Method development and validation of metformin hydrochloride in tablet dosage form. E-J Chem. 2011; 8:1309-13.
• [18]Kandagal PB, Seetharamappa J, Shaikh SMT, Manjunatha DH. Binding of trazodone hydrochloride with human serum albumin: a spectroscopic study. J Photochem Photobiol A Chem. 2007; 185:239-44.
• [19]Sun SF, Zhou B, Hou HN, Liu Y, Xiang GY. Studies on the interaction between Oxaprozin-E and bovine serum albumin by spectroscopic methods. Int J Biol Macromol. 2006; 39:197-200.
• [20]Ross PD, Subramanian S. Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry. 1981; 20:3096-102.
• [21]Li D, Zhu J, Jin J, Yao X. Studies on the binding of nevadensin to human serum albumin by molecular spectroscopy and modeling. J Mol Str. 2007; 846:34-41.
• [22]Sultana S, Bin Sayeed MS, Ahamed MU, Islam MS, Bahar A, Sultan MZ et al.. Interaction of nalbuphine hydrochloride with deoxyribonucleic acid measured by fluorescence quenching. Drug Res (Stuttg). 2013; 63:224-7.
• [23]Rabbi SNI, Sultan MZ, Sohel MD, Sultan MZ. Study of interaction between febuxostat and bovine serum albumin by fluorescence spectroscopy. J Bioanal Biomed. 2015; 7:164-70.
• [24]Rashid MA, Rabbi SNI, Sultana T, Sultan MZ, Sultan MZ. Fluorescence spectroscopic study of interaction between olanzapine and bovine serum albumin. Pharm Anal Acta. 2015; 6:408.
• [25]Koly SF, Sultan MZ, Rahman A, Kabir S, Amran MS. An in vitro study of binding of aceclofenac and pantoprazole with bovine serum albumin by UV spectroscopic method. J Pharm Sci Emerg Drugs. 2015; 3:2.