Interaction of toxic azo dyes with heme protein: Biophysical insights into the binding aspect of the food additive amaranth with human hemoglobin

Journal of Hazardous Materials

Volumn 289, Issue , 2015, Pages 204-209

  Basu, Anirban ^a   Kumar, Gopinatha Suresh ^a  

^a INDIAN INSTITUTE OF CHEMICAL BIOLOGY   (India)

Author keywords

Amaranth; Binding; Hemoglobin; Spectroscopy; Thermodynamics

Indexed keywords

AMINO ACIDS; AZO DYES; BINDING ENERGY; DICHROISM; FLUORESCENCE; FOOD ADDITIVES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; PROTEINS; SPECTROSCOPY; THERMODYNAMICS;

AMARANTH; BINDING; BIOPHYSICAL STUDIES; CONFORMATIONAL CHANGE; ENTROPIC CONTRIBUTIONS; SPECTROFLUORIMETRIC; SYNCHRONOUS FLUORESCENCE; TRYPTOPHAN RESIDUES;

HEMOGLOBIN;

AMARANTH; HEMOGLOBIN; TRYPTOPHAN; TYROSINE; AZO COMPOUND; FOOD DYE; HEMOPROTEIN;

DYE; ENTHALPY; FTIR SPECTROSCOPY; HEMOGLOBIN; PROTEIN; THERMODYNAMICS; THREE-DIMENSIONAL MODELING; TOXICITY; ULTRAVIOLET RADIATION;

ABSORPTION SPECTROSCOPY; ARTICLE; CALORIMETRY; CHEMICAL STRUCTURE; CIRCULAR DICHROISM; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; DIFFERENTIAL SCANNING CALORIMETRY; ENERGY TRANSFER; ENVIRONMENTAL CHANGE; FLUORESCENCE SPECTROSCOPY; HUMAN; INFRARED SPECTROSCOPY; ISOTHERMAL TITRATION CALORIMETRY; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; THERMOSTABILITY; X RAY CRYSTALLOGRAPHY; BIOPHYSICS; CHEMISTRY; SPECTROFLUOROMETRY; ULTRAVIOLET SPECTROPHOTOMETRY;

AMARANTHUS CAUDATUS;

AMARANTH DYE; AZO COMPOUNDS; BIOPHYSICS; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; FOOD COLORING AGENTS; HEMEPROTEINS; HEMOGLOBINS; HUMANS; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 84923301255     PISSN: 03043894     EISSN: 18733336     Source Type: Journal    
DOI: 10.1016/j.jhazmat.2015.02.044     Document Type: Article

References (42)

1. Puvaneswari N., Muthukrishnan J., Gunasekaran P. Toxicity assessment and microbial degradation of azo dyes. Indian J. Exp. Biol. 2006, 44:618-626.
2. King-Thom C. Mutagenicity and carcinogenicity of aromatic amines metabolically produced from azo dyes. J. Environ. Sci. Health C 2000, 18:51-74.
3. Yue Y., Chen X., Qin J., Yao X. A study of the binding of C. I. direct yellow 9 to human serum albumin using optical spectroscopy and molecular modeling. Dyes Pigments 2008, 79:176-182.
4. Ding F., Li N., Han B., Liu F., Zhang L., Sun Y. The binding of C.I. acid red 2 to human serum album: determination of binding mechanism and binding site using fluorescence spectroscopy. Dyes Pigm. 2009, 83:249-257.
5. Wang Y.Q., Zhang H.M., Tang B.P. The interaction of C.I. acid red 27 with human hemoglobin in solution. J. Photochem. Photobiol. B 2010, 100:76-83.
6. Lu D., Zhao X., Zhao Y., Zhang B., Zhang B., Geng M., Liu R. Binding of sudan II and sudan IV to bovine serum album: comparison studies. Food Chem. Toxicol. 2011, 49:3158-3164.
7. Wang Y.-Q., Zhang H.-M. Investigations on the binding of human hemoglobin with orange I and orange II. J. Photochem. Photobiol. B 2012, 113:14-21.
8. Zhang G., Ma Y. Mechanistic and conformational studies on the interaction of food dye amaranth with human serum albumin by multispectroscopic methods. Food Chem. 2013, 136:442-449.
9. Basu A., Suresh Kumar G. Targeting proteins with toxic azo dyes: a microcalorimetric characterization of the interaction of the food colorant amaranth with serum proteins. J. Agric. Food Chem. 2014, 62:7955-7962.
10. Basu A., Suresh Kumar G. Study on the interaction of the toxic food additive carmoisine with serum albumins: a microcalorimetric investigation. J. Hazard. Mater. 2014, 273:200-206.
11. Mpountoukas P., Pantazaki A., Kostareli E., Christodoulou P., Kareli D., Poliliou S., Mourelatos C., Lambropoulou V., Lialiaris T. Cytogenetic evaluation and DNA interaction studies of the food colorants amaranth, erythrosine and tartrazine. Food Chem. Toxicol. 2010, 48:2934-2944.
12. Ishidate M., Sofuni T., Yoshikawa K., Hayashi M., Nohmi T., Sawada M., Matsuoka A. Primary mutagenicity screening of food additives currently used in Japan. Food Chem. Toxicol. 1984, 22:623-636.
13. Nevado J.J.B., Cabanillas C.G., Salcedo A.M.C. Simultaneous spectrophotometric determination of three food dyes by using the first derivative of ratio spectra. Talanta 1995, 42:2043-2051.
14. Tsuda S., Murakami M., Matsusaka N., Kano K., Taniguchi K., Sasaki Y.F. DNA damage induced by red food dyes orally administered to pregnant and male mice. Toxicol. Sci. 2001, 61:92-99.
15. Perutz M.F., Rossmann M.G., Cullis A.F., Muirhead H., Will G., North A.C.T. Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5-Å. resolution, obtained by X-ray analysis. Nature 1960, 185:416-422.
16. Perutz M.F. X-ray analysis of hemoglobin. Science 1963, 140:863-869.
17. Peng W., Ding F., Peng Y.-K., Sun Y. Molecular recognition of malachite green by hemoglobin and their specific interactions: insights from in silico docking and molecular spectroscopy. Mol. Biosyst. 2014, 10:138-148.
18. Chatterjee S., Suresh Kumar G. Targeting the heme proteins hemoglobin and myoglobin by janus green blue and study of the dye-protein association by spectroscopy and calorimetry. RSC Adv. 2014, 4:42706-42715.
19. Hazra S., Suresh Kumar G. Structural and thermodynamic studies on the interaction of iminium and alkanolamine forms of sanguinarine with hemoglobin. J. Phys. Chem. B 2014, 118:3771-3784.
20. Hazra S., Hossain M., Suresh Kumar G. Binding of isoquinoline alkaloids berberine, palmatine and coralyne to hemoglobin: structural and thermodynamic characterization studies. Mol. Biosyst. 2013, 9:143-153.
21. Basu A., Suresh Kumar G. Interaction of the dietary pigment curcumin with hemoglobin: energetics of the complexation. Food Funct. 2014, 5:1949-1955.
22. Murakami K. Equilibrium and kinetic studies of the binding of tri- and tetra-anionic ligands to bovine serum albumin. Biophys. Chem. 1991, 41:253-261.
23. Benesi H.A., Hildebrand J.H. A spectrophotometric investigation of the interaction of iodine with aromatic hydrocarbons. J. Am. Chem. Soc. 1949, 71:2703-2707.
24. Venkateshrao S., Manoharan P.T. Conformational changes monitored by fluorescence study on reconstituted hemoglobins. Spectrochim. Acta A 2004, 60:2523-2526.
25. Mueser T.C., Rogers P.H., Arnone A. Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin. Biochemistry 2000, 39:15353-15364.
26. Alpert D.M., Jameson, Weber G. Tryptophan emission from human hemoglobin and its isolated subunits. Photochem. Photobiol. 1980, 31:1-4.
27. Lloyd J.B.F. Synchronized excitation of fluorescence emission spectra. Nat. Phys. Sci. 1971, 231:64-65.
28. Miller J.N. Recent advances in molecular luminescence analysis. Proc. Anal. Div. Chem. Soc. 1979, 16:203-208.
29. Kang J., Liu Y., Xie M.-X., Li S., Jiang M., Wang Y.-D. Interactions of human serum albumin with chlorogenic acid and ferulic acid. Biochim. Biophys. Acta 2004, 1674:205-214.
30. Abraham D.J., Mehanna A.S., Wireko F.C., Whitney J., Thomas R.P., Orringer E.P. Vanillin, a potential agent for the treatment of sickle cell anemia. Blood 1991, 77:1334-1341.
31. Safo M.K., Moure C.M., Burnett J.C., Joshi G.S., Abraham D.J. High-resolution crystal structure of deoxy hemoglobin complexed with a potent allosteric effector. Protein Sci. 2001, 10:951-957.
32. Syakhovich V.E., Parul D.A., Ruta E.Y., Bushuk B.A., Bokut S.B. 1,8-Anilinonaphthalene sulfonate binds to central cavity of human hemoglobin. Biochem. Biophys. Res. Commun. 2004, 317:761-767.
33. Cheng H., Liu H., Bao W., Zou G. Studies on the interaction between docetaxel and human hemoglobin by spectroscopic analysis and molecular docking. J. Photochem. Photobiol. B 2011, 105:126-132.
34. Khan S.N., Islam B., Yennamalli R., Zia Q., Subbarao N., Khan A.U. Characterization of doxorubicin binding site and drug induced alteration in the functionally important structural state of oxyhemoglobin. J. Pharm. Biomed. Anal. 2008, 48:1096-1104.
35. Mandal P., Ganguly T. Fluorescence spectroscopic characterization of the interaction of human adult hemoglobin and two isatins, 1-methylisatin and 1-phenylisatin: a comparative study. J. Phys. Chem. B 2009, 113:14904-14913.
36. Mahato M., Pal P., Tah B., Ghosh M., Talapatra G.B. Study of silver nanoparticle-hemoglobin interaction and composite formation. Colloids Surf. B Biointerfaces 2011, 88:141-149.
37. Chen Y.H., Yang J.T., Martinez H.M. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 1972, 11:4120-4131.
38. Lu Z.X., Cui T., Shi Q.L. Molecular Biology: Applications of Circular Dichroism and Optical Rotatory Dispersion 1987, Science Press, Beijing. 1st ed.
39. Spolar R.S., Record M.T. Coupling of local folding to site-specific binding of proteins to DNA. Science 1994, 263:777-784.
40. O'Brien R., DeDecker B., Fleming K.G., Sigler P.B., Ladbury J.E. The effects of salt on the TATA binding protein-DNA interaction from a hyperthermophilic archaeon. J. Mol. Biol. 1998, 279:117-125.
41. Basu A., Suresh Kumar G. Elucidating the energetics of the interaction of non-toxic dietary pigment curcumin with human serum albumin: a calorimetric study. J. Chem. Thermodyn. 2014, 70:176-181.
42. Ha J.H., Spolar R.S., Record M.T. Role of the hydrophobic effect in stability of site-specific protein-DNA complexes. J. Mol. Biol. 1989, 209:801-816.