Environmental Science and Pollution Research

, Volume 26, Issue 1, pp 208–214 | Cite as

A biophysical probe on the binding of 2-mercaptothioazoline to bovine hemoglobin

  • Luyi Zou
  • Xiaoyue Zhang
  • Mingying Shao
  • Ruirui Sun
  • Yuting Zhu
  • Binbin Zou
  • Zhenxing Huang
  • He Liu
  • Yue TengEmail author
Research Article


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.


Hemoglobin 2-Mercaptothioazoline Spectroscopic studies Molecular modeling Binding interaction Conformation investigation 


Funding information

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).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Supplementary material

11356_2018_3405_MOESM1_ESM.doc (87 kb)
ESM 1 (DOC 87 kb)


  1. 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 408:62–68CrossRefGoogle Scholar
  2. Bao XY, Zhu ZW, Li NQ, Chen JG (2001) Electrochemical studies of rutin interacting with hemoglobin and determination of hemoglobin. Talanta 54:591–596CrossRefGoogle Scholar
  3. 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 289:204–209CrossRefGoogle Scholar
  4. Beyssen ML, Lagorce JF, Cledat D, Buxeraud J (1999) Influence of dietary iodine on drug-induced hypothyroidism in the rat. J Pharm Pharmacol 51:745–750CrossRefGoogle Scholar
  5. 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 44:1285–1291CrossRefGoogle Scholar
  6. 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 43:1932–1937CrossRefGoogle Scholar
  7. 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 43:6935–6942CrossRefGoogle Scholar
  8. 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 56:133–140CrossRefGoogle Scholar
  9. Chi ZX, Liu RT, Yang BJ, Zhang H (2010) Toxic interaction mechanism between oxytetracycline and bovine hemoglobin. J Hazard Mater 180:741–747CrossRefGoogle Scholar
  10. Chi Z, Li S, Wen Z, Shan Y (2017) Mechanism of the toxicological interactions of decabrominated diphenyl ether with hemoglobin. Spectrosc Lett 50:381–386CrossRefGoogle Scholar
  11. 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 32:1075–1084CrossRefGoogle Scholar
  12. Irwin JJ, Sterling T, Mysinger MM, Bolstad ES, Coleman RG (2012) ZINC: a free tool to discover chemistry for biology. J Chem Inf Model 52:1757–1768CrossRefGoogle Scholar
  13. 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 4:50CrossRefGoogle Scholar
  14. Khan AY, Kumar GS (2016) Probing the binding of anticancer drug topotecan with human hemoglobin: structural and thermodynamic studies. J Photochem Photobiol B 163:185–193CrossRefGoogle Scholar
  15. Lakowicz JR, Weber G (1973) Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry 12:4171–4179CrossRefGoogle Scholar
  16. Li Y, Wei H, Liu R (2014) A probe to study the toxic interaction of tartrazine with bovine hemoglobin at the molecular level. Luminescence 29:195–200CrossRefGoogle Scholar
  17. 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 136:416–422CrossRefGoogle Scholar
  18. Liu Y, Lin JJ, Chen MM, Song L (2013) Investigation on the interaction of the toxicant, gentian violet, with bovine hemoglobin. Food Chem Toxicol 58:264–272CrossRefGoogle Scholar
  19. Lloyd JBF (1971) Synchronized excitation of fluorescence emission spectra. Nat Phys Sci 231:64–65CrossRefGoogle Scholar
  20. 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 49:3158–3164CrossRefGoogle Scholar
  21. 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 30:2785–2791CrossRefGoogle Scholar
  22. 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 35:1–18Google Scholar
  23. 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 185:416–422CrossRefGoogle Scholar
  24. 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 79:1411–1417CrossRefGoogle Scholar
  25. 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 78:512–517CrossRefGoogle Scholar
  26. Ross PD, Subramanian S (1981) Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20:3096–3102CrossRefGoogle Scholar
  27. 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 496:267–277CrossRefGoogle Scholar
  28. 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 51:250–258CrossRefGoogle Scholar
  29. 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 131:43–52CrossRefGoogle Scholar
  30. 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 53:5941–5952CrossRefGoogle Scholar
  31. 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 287:252–260CrossRefGoogle Scholar
  32. 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 22:18267–18277CrossRefGoogle Scholar
  33. 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 53:206–211CrossRefGoogle Scholar
  34. 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 58:201–207CrossRefGoogle Scholar
  35. William RW (1962) Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process. J Phys Chem 66:455–458CrossRefGoogle Scholar
  36. 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 25:11431–11439CrossRefGoogle Scholar
  37. 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 113:10454–10458CrossRefGoogle Scholar
  38. 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 65:227–232CrossRefGoogle Scholar
  39. 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 118:14820–14826Google Scholar

Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2018

Authors and Affiliations

  • Luyi Zou
    • 1
    • 2
  • Xiaoyue Zhang
    • 1
  • Mingying Shao
    • 1
  • Ruirui Sun
    • 1
  • Yuting Zhu
    • 1
  • Binbin Zou
    • 1
  • Zhenxing Huang
    • 1
    • 2
    • 3
  • He Liu
    • 1
    • 2
  • Yue Teng
    • 1
    • 2
    Email author
  1. 1.School of Environmental and Civil EngineeringJiangnan UniversityWuxiPeople’s Republic of China
  2. 2.Jiangsu Key Laboratory of Anaerobic BiotechnologyJiangnan UniversityWuxiChina
  3. 3.Jiangsu Collaborative Innovation Center of Technology and Material of Water TreatmentSuzhouChina

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