Abstract
2-Mercaptothiazoline (MTZ) is broadly present in daily use as an antifungal reagent, a brightening agent, and a corrosion inhibitor. MTZ is potentially harmful for human health. Although the toxic effects of MTZ on experimental animals have been reported, the effects of MTZ on the proteins in the circulatory system at the molecular level have not been identified previously. Here, we explored the interaction of MTZ with bovine hemoglobin (BHb) in vitro using multiple spectroscopic techniques and molecular docking. In this study, the binding capacity, acting force, binding sites, molecular docking simulation, and conformational changes were investigated. MTZ quenched the intrinsic emission of BHb via the static quenching process and could spontaneously bind with BHb mainly through van der Waals forces and hydrogen bond. The computational docking visualized that MTZ bound to the β2 subunit of BHb, which further led to some changes of the skeleton and secondary structure of BHb. This research provides valuable information about the molecular mechanisms on BHb induced by MTZ and is beneficial for clarifying the toxicological actions of MTZ in blood.
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References
Abbehausen C, de Paiva REF, Formiga ALB, Corbi PP (2012) Studies of the tautomeric equilibrium of 1,3-thiazolidine-2-thione: theoretical and experimental approaches. Chem Phys 408:62–68
Bao XY, Zhu ZW, Li NQ, Chen JG (2001) Electrochemical studies of rutin interacting with hemoglobin and determination of hemoglobin. Talanta 54:591–596
Basu A, Kumar GS (2015) Interaction of toxic azo dyes with heme protein: biophysical insights into the binding aspect of the food additive amaranth with human hemoglobin. J Hazard Mater 289:204–209
Beyssen ML, Lagorce JF, Cledat D, Buxeraud J (1999) Influence of dietary iodine on drug-induced hypothyroidism in the rat. J Pharm Pharmacol 51:745–750
Chen YH, Yang JT (1971) A new approach to the calculation of secondary structures of globular proteins by optical rotatory dispersion and circular dichroism. Biochem Bioph Res Commun 44:1285–1291
Chen YH, Chang CY, Chen CC, Chiu CY, Yu YH, Chiang PC, Chang CF, Ku Y (2004a) Decomposition of 2-mercaptothiazoline in an aqueous solution by ozonation with UV radiation. Ind Eng Chem Res 43:1932–1937
Chen YH, Chang CY, Chen CC, Chiu CY, Yu YH, Chiang PC, Chang CF, Shie JL (2004b) Kinetics of ozonation of 2-mercaptothiazoline in an electroplating solution. Ind Eng Chem Res 43:6935–6942
Chen YH, Chang CY, Chen CC, Chiu CY, Yu YH, Chiang PC, Ku Y, Chen JN, Chang CF (2004c) Decomposition of 2-mercaptothiazoline in aqueous solution by ozonation. Chemosphere 56:133–140
Chi ZX, Liu RT, Yang BJ, Zhang H (2010) Toxic interaction mechanism between oxytetracycline and bovine hemoglobin. J Hazard Mater 180:741–747
Chi Z, Li S, Wen Z, Shan Y (2017) Mechanism of the toxicological interactions of decabrominated diphenyl ether with hemoglobin. Spectrosc Lett 50:381–386
Fiehn O, Wegener G, Jochimsen J, Jekel M (1998) Analysis of the ozonation of 2-Mercaptobenzothiazole in water and tannery wastewater using sum parameters, liquid-and gas chromatography and capillary electrophoresis. Water Res 32:1075–1084
Irwin JJ, Sterling T, Mysinger MM, Bolstad ES, Coleman RG (2012) ZINC: a free tool to discover chemistry for biology. J Chem Inf Model 52:1757–1768
Kamaljeet, Bansal S, SenGupta U (2017) A study of the interaction of bovine hemoglobin with synthetic dyes using spectroscopic techniques and molecular docking. Front Chem 4:50
Khan AY, Kumar GS (2016) Probing the binding of anticancer drug topotecan with human hemoglobin: structural and thermodynamic studies. J Photochem Photobiol B 163:185–193
Lakowicz JR, Weber G (1973) Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry 12:4171–4179
Li Y, Wei H, Liu R (2014) A probe to study the toxic interaction of tartrazine with bovine hemoglobin at the molecular level. Luminescence 29:195–200
Li H, Dou H, Zhang Y, Li Z, Wang R, Chang J (2015) Studies of the interaction between FNC and human hemoglobin: a spectroscopic analysis and molecular docking. Spectrochim Acta A 136:416–422
Liu Y, Lin JJ, Chen MM, Song L (2013) Investigation on the interaction of the toxicant, gentian violet, with bovine hemoglobin. Food Chem Toxicol 58:264–272
Lloyd JBF (1971) Synchronized excitation of fluorescence emission spectra. Nat Phys Sci 231:64–65
Lu D, Zhao X, Zhao Y, Zhang B, Zhang B, Geng M, Liu R (2011) Binding of Sudan II and Sudan IV to bovine serum albumin: comparison studies. Food Chem Toxicol 49:3158–3164
Morris GM, Huey R, Lindstrom W, Sanner MF, Belew RK, Goodsell DS, Olson AJ (2009) AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility. J Comput Chem 30:2785–2791
Naeeminejad S, Assaran Darban R, Beigoli S, Saberi MR, Chamani J (2016) Studying the interaction between three synthesized heterocyclic sulfonamide compounds with hemoglobin by spectroscopy and molecular modeling techniques. J Biomol Struct Dyn 35:1–18
Perutz MF, Rossmann MG, Cullis AF, Muirhead H, Will G, North AC (1960) Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5-A. resolution, obtained by X-ray analysis. Nature 185:416–422
Rabie UM, Abou-El-Wafa MH, Nassar H (2011a) Multiple and sequential charge transfer interactions occurring in situ: a redox reaction of thiazolidine-2-thione with 2,3-dichloro-5,6-dicyano-1,4-benzoquinone. Spectrochim Acta A 79:1411–1417
Rabie UM, Abou-El-Wafa MH, Nassar H (2011b) In vitro simulation of the chemical scenario of the action of an anti-thyroid drug: charge transfer interaction of thiazolidine-2-thione with iodine. Spectrochim Acta A 78:512–517
Ross PD, Subramanian S (1981) Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20:3096–3102
Rudra S, Dasmandal S, Mahapatra A (2017) Binding interaction of sodium-N-dodecanoyl sarcosinate with hemoglobin and myoglobin: physicochemical and spectroscopic studies with molecular docking analysis. J Colloid Interface Sci 496:267–277
Sengupta B, Chakraborty S, Crawford M, Taylor JM, Blackmon LE, Biswas PK, Kramer WH (2012) Characterization of diadzein-hemoglobin binding using optical spectroscopy and molecular dynamics simulations. Int J Biol Macromol 51:250–258
Shanmugaraj K, Anandakumar S, Ilanchelian M (2014) Exploring the biophysical aspects and binding mechanism of thionine with bovine hemoglobin by optical spectroscopic and molecular docking methods. J Photochem Photobiol B 131:43–52
Solmaz R, Kardas G, Culha M, Yazici B, Erbil M (2008) Investigation of adsorption and inhibitive effect of 2-mercaptothiazoline on corrosion of mild steel in hydrochloric acid media. Electrochim Acta 53:5941–5952
Sreerama N, Woody RW (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 287:252–260
Sun H, Cui E, Liu R (2015) Molecular mechanism of copper-zinc superoxide dismutase activity change exposed to N-acetyl-L-cysteine-capped CdTe quantum dots-induced oxidative damage in mouse primary hepatocytes and nephrocytes. Environ Sci Pollut Res Int 22:18267–18277
Tan S, Wang D, Chi Z, Li W, Shan Y (2017) Study on the interaction between typical phthalic acid esters (PAEs) and human haemoglobin (hHb) by molecular docking. Environ Toxicol Pharmacol 53:206–211
Thomes JC, Comby F, Lagorce JF, Buxeraud J, Raby C (1992) Sites of ation of 2-tiazoline-2-tiol on bogenesis of tyroid-hrmones. Jpn J Pharmacol 58:201–207
William RW (1962) Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process. J Phys Chem 66:455–458
Xu M, Zhang R, Song W, Zong W, Liu R (2018) Probing the toxic mechanism of bisphenol a with acid phosphatase at the molecular level. Environ Sci Pollut Res Int 25:11431–11439
Yang QQ, Liang JG, Han HY (2009) Probing the interaction of magnetic iron oxide nanoparticles with bovine serum albumin by spectroscopic techniques. J Phys Chem B 113:10454–10458
Yang B, Hao F, Li J, Wei K, Wang W, Liu R (2014) Characterization of the binding of chrysoidine, an illegal food additive to bovine serum albumin. Food Chem Toxicol 65:227–232
Zhang H, Liu Y, Liu R, Liu C, Chen Y (2014) Molecular mechanism of lead-induced superoxide dismutase inactivation in zebrafish livers. J Phys Chem B 118:14820–14826
Funding
The work was financially supported by National Nature Science Foundation of China (NSFC 21307043, 21577083, 21506076), National Science and Technology Major Project (2017ZX07203001), China Postdoctoral Science Foundation (2016 M590411), and Jiangsu Province Postdoctoral Research Funding Scheme (1601230C).
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Zou, L., Zhang, X., Shao, M. et al. A biophysical probe on the binding of 2-mercaptothioazoline to bovine hemoglobin. Environ Sci Pollut Res 26, 208–214 (2019). https://doi.org/10.1007/s11356-018-3405-0
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DOI: https://doi.org/10.1007/s11356-018-3405-0