Insights into the binding of ferulic acid to the thermally treated xanthine oxidase

Luminescence

Volumn 31, Issue 6, 2016, Pages 1259-1266

  Dumitrascu, Loredana ^a   Stănciuc, Nicoleta ^a   Bahrim, Gabriela Elena ^a   Aprodu, Iuliana ^a  

^a DUNAREA DE JOS UNIVERSITY OF GALATI   (Romania)

Author keywords

binding; ferulic acid; fluorescence measurement; structural changes; xanthine oxidase

Indexed keywords

ASSOCIATION REACTIONS; BIOACTIVITY; COPYRIGHTS; FLUORESCENCE QUENCHING; FLUORESCENCE SPECTROSCOPY; HYDROGEN BONDS; MOLECULES; PROTEINS; SPECTROSCOPIC ANALYSIS; TEMPERATURE; VAN DER WAALS FORCES;

BINDING; BINDING CONSTANT; BINDING-SITES; BIOLOGICALLY ACTIVE COMPOUNDS; FERULIC ACIDS; FLUORESCENCE MEASUREMENTS; FOOD INDUSTRIES; STRUCTURAL CHANGE; THERAPEUTIC EFFECTS; XANTHINE OXIDASE;

BINDING SITES;

EID: 84975769725     PISSN: 15227235     EISSN: 15227243     Source Type: Journal    
DOI: 10.1002/bio.3099     Document Type: Article

References (38)

1. Fleming J, Kuchta K, Arnhold J, Rauwald Hw. Olea europaea leaf (pH.eur.) extract as well as several of its isolated phenolics inhibit the gout-related enzyme xanthine oxidase. Phytomedicine 2011;8:561–6.
2. Zhou Y, Liao J, Du F, Liung Yi. Thermodynamics of the interaction of xanthine oxidase with superoxide dismutase studied by isothermal titration calorimetry and fluorescence spectroscopy. Thermochim Acta 2005;426:173–8.
3. Campbell R, Drake M. Invited review: the effect of native and nonnative enzymes on the flavor of dried dairy ingredients. J Dairy Sci 2013;98:4773–83.
4. Masuda T, Shingai Y, Takahashi C, Inai M, Miura Y, Honda S, Masuda A. Identification of a potent xanthine oxidase inhibitor from oxidation of caffeic acid. Free Radical Bio Med 2014;69:300–7.
5. Zhao Z, Moghadasian M. Chemistry, natural sources, dietary intake and pharmacokinetic properties of ferulic acid: a review. Food Chem 2008;109:691–702.
6. Kumar N, Pruthi V. Potential applications of ferulic acid from natural sources. Biotechnol Rep 2014;4:86–93.
7. Maoka T, Tanimoto F, Sano M, Tsurukawa K, Tsuno T, Tsujiwaki S, Ishimaru K, Takii K. Effects of dietary supplementation of ferulic acid and gammaoryzanol on integument color and suppression of oxidative stress in cultured red sea bream, Pagrus major. J Oleo Sci 2008;57:133–40.
8. Lin F, Lin J, Gupta R, Tournas J, Burch J, Selim M, Monteiro-Riviere N, Grichnik J, Zielinski J, Pinnell S. Ferulic acid stabilizes a solution of vitamins C and E and doubles its photoprotection of skin. J Invest Dermatol 2005;125:826–32.
9. Itagaki S, Kurokawa T, Nakata C, Saito Y, Oikawa S, Kobayashi M, Hirano T, Iseki K. In vitro and in vivo antioxidant properties of ferulic acid: a comparative study with other natural oxidation inhibitors. Food Chem 2009;114:466–71.
10. Adam A, Crespy V, Levrat-Verny A, Leenhardt F, Leuillet M, Demigné C, Remesy C. The bioavailability of ferulic acid is governed primarily by the food matrix rather than its metabolism in intestine and liver in rats. J Nutr 2002;132:1962–8.
11. Yan J, Zhang G, Hu Y, Ma Y. Effect of luteolin on xanthine oxidase: Inhibition kinetics and interaction mechanism merging with docking simulation. Food Chem 2013;141:3766–73.
12. Pauff J, Hille R. Inhibition studies on bovine xanthine oxidase by luteolin, silibinin, quercitin, and curcumin. J Nat Prod 2009;72:725–31.
13. Rasoulzadeh F, Jabary H, Naseri A, Reza Rashidi M. Fluorescence quenching study of quercitin interaction with bovine milk xanthine oxidase. Spectrochim Acta A 2009;72:190–3.
14. Masuoka N, Nihei K, Maeta A, Yamagiwa Y, Kubo I. Inhibitory effects of cardols and related compounds on superoxide anion generation by xanthine oxidase. Food Chem 2015;166:270–4.
15. Wang F, Yang L, Huang K, Li X, Hao X, Stöckigta J, Zhao Y. Preparation of ferulic acid derivatives and evaluation of their xanthine oxidase inhibition activity. Nat Prod Lett 2007;21:196–202.
16. Shen L, Xu H, Huang F, Li Y, Xiao J, Xiao H, Ying M, Tian S, Yang Z, Liu G, Hua Z, He Z, Zhou K. Study on interaction of ligupurpuroside A with bovine serum albumin by multi-spectroscopic methods. J Lumin 2014;154:80–8.
17. Zhao X, Hao F, Lu D, Liu W, Zhou Q, Jiang G. Influence of the surface functional group density on the carbon-nanotube-induced α-chymotrypsin structure and activity alterations. ACS Applied Materials & Interfaces 2015;7:18880–90.
18. Zhao X, Liu R, Chi Z, Teng Y, Qin P. New insights into the behavior of bovine serum albumin adsorbed onto carbon nanotubes: comprehensive spectroscopic studies. J Phys Chem B. 2010;114:5625–31.
19. Dumitrascu L, Stănciuc N, Ciumac A, Bahrim G, Aprodu I. pH and heat-dependent behaviour of glucose oxidase down to single molecule level by combined fluorescence spectroscopy and molecular modeling. J Sci Food Agr 2015. DOI:10.1002/jsfa.7296.
20. Ishikita H, Eger T, Okamoto K, Nishino T, Pai E. Protein conformational gating of enzymatic activity in xanthine oxidoreductase. J Am Chem Soc 2011;134:999–1009.
21. Hess B, Kutzner C, van der Spoel D, Lindahl E. GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 2008;4:435–47.
22. Schneidman-Duhovny D, Inbar Y, Nussinov R, Wolfson H. PatchDock and SymmDock: servers for rigid and symmetric docking. Nucleic Acids Res 2005;33:363–7.
23. Andrusier N, Nussinov R, Wolfson H. FireDock: fast interaction refinement in molecular docking. Proteins 2007;69:139–59.
24. Zhao X, Lua D, Hao F, Liu R. Exploring the diameter and surface dependent conformational changes in carbon nanotube-protein corona and the related cytotoxicity. J Hazard Mater 2015;292:98–107.
25. Sarzehi S, Chamani J. Investigation on the interaction between tamoxifen and human holo-transferrin: determination of the binding mechanism by fluorescence quenching, resonance light scattering and circular dichroism methods. Int J Biol Macromol 2010;47:558–69.
26. Lakowicz J. Principles of fluorescence spectroscopy. 3rd ed. New York: Springer Publications, 2006;237–65.
27. + and bovine serum albumin: a spectroscopic investigation. Sci Total Environ 2011;409:892–7.
28. Rub M, Khan J, Asiri A, Khan R. ud-Din K. Study on the interaction between amphiphilic drug and bovine serum albumin. A thermodynamic and spectroscopic description. J Lumin 2014;155:39–46.
29. Fan X, Zhang Y, Wang J, Yang L, Jiang F, Liu Y. Exploring the interaction between rotenone and human serum albumin. J Chem Thermodyn 2014;69:186–92.
30. Li H, Pu J, Wang Y, Liu C, Yu J, Li T, Wang R. Comparative study of the binding of trypsin with bifendate and analogs by spectrofluorimetry. Spectrochim Acta A 2013;115:1–11.
31. Li D, Zhang T, Ji B. Influences of pH, urea and metal ions on the interaction of sinomenine with Lysozyme by steady state fluorescence spectroscopy. Spectrochim Acta A 2014;130:440–6.
32. Meti D, Byadagi S, Nandibewoor S, Chimatadar A. Multi-spectral characterization & effect of metal ions on the binding of bovine serum albumin upon interaction with a lincosamide antibiotic drug, clindamycin phosphate. J Photochem Photobiol B 2014;138:324–30.
33. Shen L, Ji H. Bioorg. Insights into the inhibition of xanthine oxidase by curcumin. Med Chem Lett 2009;19:5990–3.
34. Bani-Yaseen A. Spectrofluorimetric study on the interaction between antimicrobial drug sulfamethazine and bovine serum albumin. J Lumin 2011;13:1042–7.
35. Bartolomé B, Estrella I, Hernández M. Interaction of low molecular weight phenolics with proteins (BSA). J Food Sci 2000;65:617–21.
36. Krissinel E. Crystal contacts as nature's docking solutions. J Comput Chem 2010;31:133–43.
37. Li S, Huang K, Zhong M, Guoa J, Wang W, Zhu R. Comparative studies on the interaction of caffeic acid, chlorogenic acid and ferulic acid with bovine serum albumin. Spectrochim Acta A 2010;77:680–6.
38. Sattar Z, Iranfar H, Asoodeh A, Saberi M, Mazhari M, Chamani J. Interaction between holo transferrin and HSA–PPIX complex in the presence of lomefloxacin: an evaluation of PPIX aggregation in protein–protein interactions. Spectrochim Acta A Mol Biomol Spectrosc 2012;97:1089–100.