Abstract
The interaction between juglone at the concentration range of 10–110 µM and bovine serum albumin (BSA) or human serum albumin (HSA) at the constant concentration of 11 µM was investigated by fluorescence and UV absorption spectroscopy under physiological-like condition. Performing the experiments at different temperatures showed that the fluorescence intensity of BSA/HSA was decreased in the presence of juglone by a static quenching mechanism due to the formation of the juglone–protein complex. The binding constant for the interaction was in the order of 103 M−1, and the number of binding sites for juglone on serum albumins was determined to be equal to one. The thermodynamic parameters including enthalpy (ΔH), entropy (ΔS) and Gibb’s free energy (ΔG) changes were obtained by using the van’t Hoff equation. These results indicated that van der Waals force and hydrogen bonding were the main intermolecular forces stabilizing the complex in a spontaneous association reaction. Moreover, the interaction of BSA/HSA with juglone was verified by UV absorption spectra and molecular docking. The results of synchronous fluorescence, UV–visible and CD spectra demonstrated that the binding of juglone with BSA/HSA induces minimum conformational changes in the structure of albumins. The increased binding affinity of juglone to albumin observed in the presence of site markers (digoxin and ibuprofen) excludes IIA and IIIA sites as the binding site of juglone. This is partially in agreement with the results of molecular docking studies which suggests sub-domain IA of albumin as the binding site.
Similar content being viewed by others
References
M.J. Nirmala, A. Samundeeswari, P.D. Sankar, Res. Plant Biol. 1, 01 (2011)
A. Anantharaman, B. Subramanian, R. Chandrasekaran, R. Seenivasan, R. Siva, Ind. Crops Prod. 53, 167 (2014)
D.J. Newman, G.M. Cragg, K.M. Snader, J. Nat. Prod. 66, 1022 (2003)
G. Schwartsmann, Ann. Oncol. 11, 235 (2000)
J.D. McChesney, S.K. Venkataraman, J.T. Henri, Phytochemistry 68, 2015 (2007)
D.A. Dias, S. Urban, U. Roessner, Metabolites 2, 303 (2012)
J. Krause, G. Tobin, in Using Old Solutions to New Problems-natural Drug Discovery in the 21st Century, ed. by M. Kulka (InTech, Croatia, 2013), p. 3–35
N. Balasundram, K. Sundram, S. Samman, Food Chem. 99, 191 (2006)
J. Inbaraj, C. Chignell, Chem. Res. Toxicol. 17, 55 (2004)
V. Akbari, R. Jamei, R. Heidari, A. Jahanban Esfahlan, Food Chem. 135, 2404 (2012)
L. Duroux, F.M. Delmotte, J.-M. Lancelin, G. Keravis, C. Jay-Allemand, Biochem. J. 333, 275 (1998)
N. Cenas, S. Prast, H. Nivinskas, J. Sarlauskas, E.S. Arnér, J. Biol. Chem. 281, 5593 (2006)
E. Dičkancaité, N. Čénas, A. Kalvelyté, N. Serapiniené, Biochem. Mol. Biol. Int. 41, 987 (1997)
H. Kamei, T. Koide, T. Kojima, Y. Hashimoto, M. Hasegawa, Cancer Biother. Radiopharma. 13, 185 (1998)
J.F. Rippmann, S. Hobbie, C. Daiber, B. Guilliard, M. Bauer, J. Birk, H. Nar, P. Garin-Chesa, W.J. Rettig, A. Schnapp, Cell Growth Differ. Mol. Biol. J. Am. Assoc. Cancer Res. 11, 409 (2000)
J. Segura-Aguilar, K. Jönsson, U. Tidefelt, C. Paul, Leuk. Res. 16, 631 (1992)
P. Babula, V. Adam, R. Kizek, Z. Sladký, L. Havel, Environ. Exp. Bot. 65, 330 (2009)
S. Sugie, K. Okamoto, K. Rahman, T. Tanaka, K. Kawai, J. Yamahara, H. Mori, Cancer Lett. 127, 177 (1998)
H.L. Xu, X.F. Yu, S.C. Qu, X.R. Qu, Y.F. Jiang, D.Y. Sui, Food Chem. Toxicol. 50, 590 (2012)
B. Kiran Aithal, M. Sunil Kumar, B. Nageshwar Rao, N. Udupa, B. Satish Rao, Cell Biol. Int. 33, 1039 (2009)
Y.-B. Ji, Z.-Y. Qu, X. Zou, Exp. Toxicol. Pathol. 63, 69 (2011)
H. Wang, Y. Mao, A.Y. Chen, N. Zhou, E.J. LaVoie, L.F. Liu, Biochemistry 40, 3316 (2001)
S.-H. Chao, A.L. Greenleaf, D.H. Price, Nucleic Acids Res. 29, 767 (2001)
M.T. Paulsen, M. Ljungman, Toxicol. Appl. Pharmacol. 209, 1 (2005)
J.J. Lohman, F.W. Merkus, K. Rahn, Pharm. World Sci. 8, 302 (1986)
A. Sułkowska, J. Mol. Struct. 614, 227 (2002)
B. Elsadek, F. Kratz, J. Control. Release 157, 4 (2012)
P.A. Zunszain, J. Ghuman, T. Komatsu, E. Tsuchida, S. Curry, BMC Struct. Biol. 3, 6 (2003)
A. Jahanban-Esfahlan, V. Panahi-Azar, S. Sajedi, Biopolymers 103, 638 (2015)
F. Kratz, J. Control. Release 132, 171 (2008)
A.O. Elzoghby, W.M. Samy, N.A. Elgindy, J. Control. Release 157, 168 (2012)
J.R. Lakowicz, Principles of Fluorescence Spectroscopy (Springer, New York, 2006)
S. Li, D. Yao, H. Bian, Z. Chen, J. Yu, Q. Yu, H. Liang, J. Solut. Chem. 40, 709 (2011)
F. Samari, M. Shamsipur, B. Hemmateenejad, T. Khayamian, S. Gharaghani, Eur. J. Med. Chem. 54, 255 (2012)
A. Belatik, S. Hotchandani, J. Bariyanga, H. Tajmir-Riahi, Eur. J. Med. Chem. 48, 114 (2012)
A. Thompson Mark, ArgusLab 4.0.1 (Planaria Software LLC, Seattle, WA, 2004)
J.R. Lakowicz, G. Weber, Biochemistry 12, 4161 (1973)
S. Lehrer, Biochemistry 10, 3254 (1971)
D. Leckband, Annu. Rev. Biophys. Biomol. Struct. 29, 1 (2000)
P.D. Ross, S. Subramanian, Biochemistry 20, 3096 (1981)
B. Valeur, Molecular Fluorescence: Principles and Applications (Wiley, New York, 2001)
G.-F. Shen, T.-T. Liu, Q. Wang, M. Jiang, J.-H. Shi, J. Photochem. Photobiol. B 153, 380 (2015)
Y.-Q. Wang, H.-M. Zhang, G.-C. Zhang, S.-X. Liu, Q.-H. Zhou, Z.-H. Fei, Z.-T. Liu, Int. J. Biol. Macromol. 41, 243 (2007)
Y.-J. Hu, Y. Liu, X.-H. Xiao, Biomacromolecules 10, 517 (2009)
B.-M. Liu, J. Zhang, A.-J. Hao, L. Xu, D. Wang, H. Ji, S.-J. Sun, B.-Q. Chen, B. Liu, Spectrochim. Acta Part A Mol. Biomol. Spectrosc. 155, 88 (2016)
Acknowledgements
The authors would like to thank Research Office of Tabriz University of Medical Sciences for providing financial aid under Postgraduate Research Grant scheme for the Ph.D. thesis (No. 92) of AJE.
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Conflict of interest
The authors declare no conflict of interest.
Rights and permissions
About this article
Cite this article
Jahanban-Esfahlan, A., Davaran, S., Moosavi-Movahedi, A.A. et al. Investigating the interaction of juglone (5-hydroxy-1, 4-naphthoquinone) with serum albumins using spectroscopic and in silico methods. J IRAN CHEM SOC 14, 1527–1540 (2017). https://doi.org/10.1007/s13738-017-1094-0
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s13738-017-1094-0