Skip to main content
SpringerLink
Log in

Study of the Interaction Between Coenzyme Q10 and Human Serum Albumin: Spectroscopic Approach

  • Published:
Journal of Solution Chemistry Aims and scope Submit manuscript

Abstract

UV–vis absorption, fluorescence, circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopic methods were employed to reveal the mechanism of the binding between coenzyme Q10 (CoQ10) and human serum albumin (HSA) under simulated physiological conditions (pH = 7.4). The binding parameters were calculated by the fluorescence quenching method. The results demonstrate that the fluorescence quenching of HSA by CoQ10 is mainly static quenching due to the formation of HSA–CoQ10 complexes, and the number of binding sites (n) is equal to 1. The thermodynamic parameters (ΔH 0 = −43.18 kJ·mol−1, ΔS 0 = −47.05 J·mol−1·K−1, ΔG 0 = −29.15 kJ·mol−1) indicate that the enthalpy-driven binding process is favorable, and the main binding forces between CoQ10 and HSA are hydrogen bonds and van der Waals forces. The competitive experiments using different site markers indicate that subdomain IIA (site I) of HSA is the primary binding site for CoQ10. The average binding distance (r) between HSA and CoQ10 is 4.29 nm, which was estimated according to the Förster’s theory of non-radiation energy transfer. In addition, the UV–vis absorption, synchronous fluorescence, three-dimensional fluorescence, 8-anilino-1-naphthalenesulfonic acid fluorescence, CD spectra, and FT-IR spectroscopy data show slight conformational changes of HSA in the presence of CoQ10. These findings provide valuable binding information between HSA and CoQ10, which may be beneficial to pharmacokinetics research and could be used to design the dosage form of CoQ10.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7
Fig. 8
Fig. 9
Fig. 10
Fig. 11
Fig. 12
Fig. 13

Similar content being viewed by others

References

  1. Cui, F.L., Yan, Y.H., Zhang, Q.Z., Qu, G.R., Du, J., Yao, X.J.: A study on the interaction between 5-methyluridine and human serum albumin using fluorescence quenching method and molecular modeling. J. Mol. Model. 16, 255–262 (2010)

    Article  CAS  Google Scholar 

  2. Suryawanshi, V.D., Anbhule, P.V., Gore, A.H., Patil, S.R., Kolekar, G.B.: Spectroscopic investigation on the interaction pyrimidine derivative, z-amino-6-hydroxy-4-(3,4-dimethoxyphenyl)-pyrimidine-5-carbonitrile with human serum albumin: mechanistic and conformational study. Ind. Eng. Chem. Res. 51, 95–102 (2012)

    Article  CAS  Google Scholar 

  3. Tousi, S.H., Saberi, M.R., Chamani, J.: Comparing the interaction of cyclophosphamide monohydrate to human serum albumin as opposed to holo-transferrin by spectroscopic and molecular modeling methods: evidence foe allocating the binding site. Protein Pept. Lett. 17, 1524–1535 (2010)

    Article  CAS  Google Scholar 

  4. Curry, S., Mandelkow, H., Brick, P., Franks, N.: Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat. Struct. Biol. 5, 827–835 (1998)

    Article  CAS  Google Scholar 

  5. Buttar, D., Colclough, N., Gerhardt, S., MacFaul, P.A., Phillips, S.D., Plowright, A., Whittamore, P., Tam, K., Maskos, K., Steinbacher, S., Steuber, H.: A combined spectroscopic and crystallographic approach to probing drug–human serum albumin interactions. Bioorg. Med. Chem. 18, 7486–7496 (2010)

    Article  CAS  Google Scholar 

  6. Pan, X.R., Qin, P.F., Liu, R.T., Wang, J.: Characterizing the interaction between tartrazine and two serum albumins by a hybrid spectroscopic approach. J. Agric. Food Chem. 59, 6650–6656 (2011)

    Article  CAS  Google Scholar 

  7. Darwish, S.M., Abu Sharkh, S.E., Abu Teir, M.M., Makharza, S.A., Abu-hadid, M.M.: Spectroscopic investigations of pentobarbital interaction with human serum albumin. J. Mol. Struct. 963, 122–129 (2010)

    Article  CAS  Google Scholar 

  8. Zhang, W.J., Xiong, X.J., Wang, F., Ge, Y.S., Liu, Y.: Studies of the interaction between ronidazole and human serum albumin by spectroscopic and molecular docking methods. J. Solution Chem. 42, 1194–1206 (2013)

    Article  Google Scholar 

  9. Frei, B., Kim, M.C., Ames, B.N.: Ubiquinol-10 is an effective lipid-soluble antioxidant at physiological concentrations. Proc. Natl. Acad. Sci. USA 87, 4879–4883 (1990)

    Article  CAS  Google Scholar 

  10. Itagaki, S., Ochiai, A., Kobayashi, M., Sugawara, M., Hiran, T., Iseki, K.: Interaction of coenzyme Q10 with the intestinal drug transporter p-glycoprotein. J. Agric. Food Chem. 56, 6923–6927 (2008)

    Article  CAS  Google Scholar 

  11. Crane, F.L.: Biochemical functions of coenzyme Q10. J. Am. Coll. Nutr. 20, 591–598 (2001)

    Article  CAS  Google Scholar 

  12. Shults, C.W., Oakes, D., Kieburtz, K., Beal, M.F., Haas, R., Plumb, S., Juncos, J.L., Nutt, J., Shoulson, I., Carter, J., Kompoliti, K., Perlmutter, J.S., Reich, S., Stern, M., Watts, R.L., Kurlan, R., Molho, E., Harrison, M., Lew, M.: Effects of coenzyme Q10 in early Parkinson disease: evidence of slowing of the functional decline. Arch. Neurol. 59, 1541–1550 (2002)

    Article  Google Scholar 

  13. Mancini, A., Festa, R., Raimondo, S., Pontecorvi, A., Littarru, G.P.: Hormonal influence on coenzyme Q10 levels in blood plasma. Int. J. Mol. Sci. 12, 9216–9225 (2011)

    Article  CAS  Google Scholar 

  14. Stocker, R., Bowry, V.W., Frei, B.: Ubiquinol-10 protects human low density lipoprotein more efficiently against lipid peroxidation than does α-tocopherol. Proc. Natl. Acad. Sci. USA 88, 1646–1650 (1991)

    Article  CAS  Google Scholar 

  15. Mizushina, Y., Takeuchi, T., Takakusagi, Y., Yonezawa, Y., Mizuno, T., Yanagi, K.-I., Imamoto, N., Sugawara, F., Sakaguchi, K., Yoshida, H., Fujita, M.: Coenzyme Q10 as a potent compound that inhibits Cdt1–geminin interaction. BBA Gen Subj 1780, 203–213 (2008)

    Article  CAS  Google Scholar 

  16. Qiu, L., Ding, H., Wang, W., Kong, Z., Li, X., Shi, Y., Zhong, W.: Coenzyme Q(10) production by immobilized Sphingomonas sp. ZUTE03 via a conversion–extraction coupled process in a three-phase fluidized bed reactor. Enzym Microb. Technol. 50, 137–142 (2012)

    Article  CAS  Google Scholar 

  17. Dimitrova, S., Pavlova, K., Lukanov, L., Zagorchev, P.: Synthesis of coenzyme Q10 and β-carotene by yeasts isolated from antarctic soil and lichen in response to ultraviolet and visible radiations. Appl. Biochem. Biotechnol. 162, 795–804 (2010)

    Article  CAS  Google Scholar 

  18. Lipshutz, B.H., Lower, A., Berl, V., Schein, K., Wetterich, F.: An improved synthesis of the “miracle nutrient” coenzyme Q10. Org. Lett. 7, 4095–4097 (2005)

    Article  CAS  Google Scholar 

  19. Soares, S., Mateus, N., Freitas, V.D.: Interaction of different polyphenols with bovine serum albumin (BSA) and human salivary α-amylase (HSA) by fluorescence quenching. J. Agric. Food Chem. 55, 6726–6735 (2007)

    Article  CAS  Google Scholar 

  20. Mahesha, H.G., Singh, S.A., Srinivasan, N., Rao, A.G.: A spectroscopic study of the interaction of isoflavones with human serum albumin. FEBS J. 273, 451–467 (2006)

    Article  CAS  Google Scholar 

  21. Chen, T., Cao, H., Zhu, S., Lu, Y., Shang, Y., Wang, M., Tang, Y., Zhu, L.: Investigation of the binding of Salvianolic acid B to human serum albumin and the effect of metal ions on the binding. Spectrochim. Acta A 81, 645–652 (2011)

    Article  CAS  Google Scholar 

  22. Kitamura, K., Omran, A.A., Takegami, S., Tanaka, R., Kitade, T.: 19F NMR spectroscopic characterization of the interaction of niflumic acid with human serum albumin. Anal. Bioanal. Chem. 387, 2843–2848 (2007)

    Article  CAS  Google Scholar 

  23. Chi, Z., Liu, R.: Phenotypic characterization of the binding of tetracycline to human serum albumin. J. Agric. Food Chem. 12, 203–209 (2011)

    CAS  Google Scholar 

  24. Lakowicz, J.R.: Principles of Fluorescence Spectroscopy, 3rd edn, pp. 277–285. Plenum Press, New York (2006)

    Book  Google Scholar 

  25. Teng, Y., Liu, R.T., Li, C., Xia, Q., Zhang, P.J.: The interaction between 4-aminoantipyrine and bovine serum albumin: multiple spectroscopic and molecular docking investigations. J. Hazard. Mater. 190, 574–581 (2011)

    Article  CAS  Google Scholar 

  26. Wu, X., Liu, J., Huang, H., Xue, W., Yao, X., Jin, J.: Interaction studies of aristolochic acid I with human serum albumin and the binding site of aristolochic acid I in subdomain IIA. Int. J. Biol. Macromol. 49, 343–350 (2011)

    Article  CAS  Google Scholar 

  27. Hu, Y.J., Liu, Y., Xiao, X.H.: Investigation of the interaction between berberine and human serum albumin. Biomacromolecules 10, 517–521 (2009)

    Article  CAS  Google Scholar 

  28. Wang, W., Min, W., Chen, J., Wu, X., Hu, Z.: Binding study of diprophylline with lysozyme by spectroscopic methods. J. Lumin. 131, 820–824 (2011)

    Article  CAS  Google Scholar 

  29. Zhang, H., Huang, X., Zhang, M.: Spectral diagnostics of the interaction between pyridoxine hydrochloride and bovine serum albumin in vitro. Mol. Biol. Rep. 35, 699–705 (2008)

    Article  CAS  Google Scholar 

  30. Toneatto, J., Argüello, G.A.: New advances in the study on the interaction of [Cr(phen)2(dppz)]3+ complex with biological models; association to transporting proteins. J. Inorg. Biochem. 105, 645–651 (2011)

    Article  CAS  Google Scholar 

  31. Ding, F., Liu, W., Diao, J.X., Sun, Y.: Characterization of Alizarin Red S binding sites and structural changes on human serum albumin: a biophysical study. J. Hazard. Mater. 186, 352–359 (2011)

    Article  CAS  Google Scholar 

  32. Sudlow, G., Birkett, D.J., Wade, D.N.: The characterization of two specific drug binding sites on human serum albumin. Mol. Pharmacol. 11, 824–832 (1975)

    CAS  Google Scholar 

  33. Brodersen, R., Sjödin, T., Sjöholm, I.: Independent binding of ligands to human serum albumin. J. Biol. Chem. 252, 5067–5072 (1977)

    CAS  Google Scholar 

  34. Zhang, G., Wang, L., Pan, J.: Probing the binding of the flavonoid diosmetin to human serum albumin by multispectroscopic techniques. J. Agric. Food Chem. 60, 2721–2729 (2012)

    Article  CAS  Google Scholar 

  35. Zhang, G., Ma, Y.: Mechanistic and conformational studies on the interaction of food dye amaranth with human serum albumin by multispectroscopic methods. Food Chem. 136, 442–449 (2013)

    Article  CAS  Google Scholar 

  36. Lu, D., Zhao, X., Zhao, Y., Zhang, B., Geng, M., Liu, R.: Binding of Sudan II and Sudan IV to bovine serum albumin: comparison studies. Food Chem. Toxicol. 49, 3158–3164 (2011)

    Article  CAS  Google Scholar 

  37. Van de Hulst, H.C.: Light Scattering by Small Particles, pp. 383–446. Dover Publications, New York (1981)

    Google Scholar 

  38. Liu, W., Yang, T., Yao, C., Zuo, S., Kong, Y.: Spectroscopic studies on the interaction between troxerutin and bovine hemoglobin. J. Solution Chem. 42, 1169–1182 (2013)

    Article  Google Scholar 

  39. Wang, Y., Wang, X., Wang, J., Zhao, Y., He, W., Guo, Z.: Noncovalent interactions between a trinuclear monofunctional platinum complex and human serum albumin. Inorg. Chem. 50, 12661–12668 (2011)

    Article  CAS  Google Scholar 

  40. Cheng, Z., Zhang, L., Zhao, H., Liu, R., Xu, Q.: Spectroscopic investigation of the interactions of cryptotanshinone and icariin with two serum albumins. J. Solution Chem. 42, 1238–1262 (2013)

    Article  CAS  Google Scholar 

  41. Liu, M., Zhang, W., Qiu, L., Lin, X.: Synthesis of butyl–isobutyl-phthalate and its interaction with α-glucosidase in vitro. J. Biochem. 149, 27–33 (2011)

    Article  CAS  Google Scholar 

  42. Shen, H., Gu, Z., Jian, K., Qi, J.: In vitro study on the binding of gemcitabine to bovine serum albumin. J. Pharm. Biomed. Anal. 75, 86–93 (2013)

    Article  CAS  Google Scholar 

  43. Hemmateenejad, B., Shamsipur, M., Samari, F., Khayamian, T., Ebrahimi, M., Rezaei, Z.: Combined fluorescence spectroscopy and molecular modeling studies on the interaction between harmalol and human serum albumin. J. Pharm. Biomed. Anal. 67–68, 201–208 (2012)

    Article  Google Scholar 

  44. Liang, M., Liu, R., Qi, W., Su, R., Yu, Y., Wang, L., He, Z.: Interaction between lysozyme and procyanidin: multilevel structural nature and effect of carbohydrates. Food Chem. 138, 1596–1603 (2012)

    Article  Google Scholar 

  45. Chen, Y.H., Yang, J.T., Martinez, H.M.: Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry (US) 11, 4120–4131 (1972)

    Article  CAS  Google Scholar 

  46. Greenfield, N.J., Fasman, G.D.: Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry (US) 8, 4108–4116 (1969)

    Article  CAS  Google Scholar 

  47. Divsalar, A., Saboury, A.A., Haertlé, T., Sawyer, L., Mansouri-Torshizi, H., Barzegar, L.: Spectroscopic and calorimetric study of 2,2′-dibipyridin Cu(II) chloride binding to bovine β-lactoglobulin. J. Solution Chem. 43, 705–715 (2013)

    Article  Google Scholar 

  48. Zhang, G., Ma, Y., Wang, L., Zhang, Y., Zhou, J.: Multispectroscopic studies on the interaction of maltol, a food additive, with bovine serum albumin. Food Chem. 133, 264–270 (2012)

    Article  CAS  Google Scholar 

Download references

Acknowledgments

This work was supported by the Program for New Century Excellent Talents in Chinese University (NCET-08-0386), the 863 Program of China (2008AA10Z318, 2012AA06A303, 2013AA102204), the Natural Science Foundation of China (20976125, 31071509, 51173128) and Tianjin (10JCYBJC05100), the Ministry of Science and Technology of China (2012YQ090194), the Beiyang Young Scholar of Tianjin University (2012) and the Program of Introducing Talents of Discipline to Universities of China (Number B06006).

Author information

Authors and Affiliations

  1. School of Life Sciences, Tianjin University, Tianjin, 300072, People’s Republic of China

    Xin Peng

  2. Chemical Engineering Research Center, School of Chemical Engineering and Technology, Tianjin University, Tianjin, 300072, People’s Republic of China

    Xin Peng, Yinhe Sun, Wei Qi, Rongxin Su & Zhimin He

  3. State Key Laboratory of Chemical Engineering, Tianjin University, Tianjin, 300072, People’s Republic of China

    Wei Qi, Rongxin Su & Zhimin He

  4. Tianjin Key Laboratory of Membrane Science and Desalination Technology, Tianjin University, Tianjin, 300072, People’s Republic of China

    Wei Qi & Rongxin Su

  5. The Co-Innovation Center of Chemistry and Chemical Engineering of Tianjin, Tianjin, People’s Republic of China

    Wei Qi, Rongxin Su & Zhimin He

Authors
  1. Xin Peng
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Yinhe Sun
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Wei Qi
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Rongxin Su
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Zhimin He
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Wei Qi.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Peng, X., Sun, Y., Qi, W. et al. Study of the Interaction Between Coenzyme Q10 and Human Serum Albumin: Spectroscopic Approach. J Solution Chem 43, 585–607 (2014). https://doi.org/10.1007/s10953-014-0146-7

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10953-014-0146-7

Keywords

Search

Navigation