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 AiM  Vol.9 No.1 , January 2019
Fluorescence Spectroscopy and Molecular Docking Approach to Probe the Interaction between Dehydroeburicoic Acid and Human Serum Albumin
Abstract: The interaction between dehydroeburicoic acid (DeEA), a triterpene purified from medicinal fungi and the major transport protein, human serum albumin (HSA), were systematically studied by fluorescence spectroscopy, synchronous fluorescence spectroscopy, three-dimensional fluorescence spectroscopy and molecular docking approach under simulated physiological conditions. The intrinsic fluorescence of HSA was quenched through the combination of static and dynamic quenching mechanism. DeEA cannot be stored and carried by HSA in the body at higher temperature. The hydrogen bonding, hydrophobic force and van der Waals force were major acting forces. The site II was the major binding site. The energy transfer could occur with high probability and the binding distance was 3.29 nm. The binding process slightly changed the conformation and microenvironment of HSA. The DeEA molecule entered the hydrophobic cleft of HSA and formed the hydrogen bonding with Glu-492 and Lys-545.
Cite this paper: Zheng, S. , Yang, S. , Cheng, X. , Bau, T. , Li, Y. , Zhang, R. and Bao, H. (2019) Fluorescence Spectroscopy and Molecular Docking Approach to Probe the Interaction between Dehydroeburicoic Acid and Human Serum Albumin. Advances in Microbiology, 9, 21-37. doi: 10.4236/aim.2019.91003.
References

[1]   Gascoigne, R.M., Robertson, A. and Simes, J.J.H. (1953) The Chemistry of Fungi. Part XVII. Dehydroeburicoic Acid. Journal of the Chemical Society, 6, 1830-1837.
https://doi.org/10.1039/jr9530001830

[2]   Deng, J., Chen, S., Jow, G., Hsueh, C. and Jeng, C. (2009) Dehydroeburicoic Acid Induces Calcium- and Calpain-Dependent Necrosis in Human U87MG Glioblastomas. Chemical Research in Toxicology, 22, 1817-1826.
https://doi.org/10.1021/tx9002275

[3]   Guan-Jhong, H., Jeng-Shyan, D., Shyh-Shyun, H., Chao-Ying, L., Wen-Chi, H., Sheng-Yang, W., Ping-Jyun, S. and Yueh-Hsiung, K. (2013) Hepatoprotective Effects of Eburicoic Acid and Dehydroeburicoic Acid from Antrodia camphorata in a Mouse Model of Acute Hepatic Injury. Food Chemistry, 141, 3020-3027.
https://doi.org/10.1016/j.foodchem.2013.03.061

[4]   Deng, J.S., Huang, S.S., Lin, T.H., Lee, M.M., Kuo, C.C., Sung, P.J., Hou, W.C., Huang, G.J. and Kuo, Y.H. (2013) Analgesic and Anti-Inflammatory Bioactivities of Eburicoic Acid and Dehydroeburicoic Acid Isolated from Antrodia camphorata on the Inflammatory Mediator Expression in Mice. Journal of Agricultural and Food Chemistry, 61, 5064-5071.
https://doi.org/10.1021/jf303820k

[5]   Du, Y.C., Chang, F.R., Wu, T.Y., Hsu, Y.M., El-Shazly, M., Chen, C.F., Sung, P.J., Lin, Y.Y., Lin, Y.H., Wu, Y.C. and Lu, M.C. (2012) Antileukemia Component, Dehydroeburicoic Acid from Antrodia camphorata Induces DNA Damage and Apoptosis in Vitro and in Vivo Models. Phytomedicine, 19, 788-796.
https://doi.org/10.1016/j.phymed.2012.03.014

[6]   Kuo, Y.H., Lin, C.H. and Shih, C.C. (2016) Dehydroeburicoic Acid from Antrodia camphorata Prevents the Diabetic and Dyslipidemic State via Modulation of Glucose Transporter 4, Peroxisome Proliferator-Activated Receptor Alpha Expression and AMP-Activated Protein Kinase Phosphorylation in High-Fat-Fed Mice. International Journal of Molecular Sciences, 17, 872.
https://doi.org/10.3390/ijms17060872

[7]   Kuo, Y.H., Lin, C.H. and Shih, C.C. (2015) Antidiabetic and Antihyperlipidemic Properties of a Triterpenoid Compound, Dehydroeburicoic Acid, from Antrodia camphorata in Vitro and in Streptozotocin-Induced Mice. Journal of Agricultural and Food Chemistry, 63, 10140-10151.
https://doi.org/10.1021/acs.jafc.5b04400

[8]   Azzazy, H.M.E. and Christenson, R.H. (1997) All about Albumin: Biochemistry, Genetics, and Medical Applications. American Association for Clinical Chemistry Inc., 432-450.

[9]   Shaw, A.K. and Pal, S.K. (2008) Resonance Energy Transfer and Ligand Binding Studies on pH-Induced Folded States of Human Serum Albumin. Journal of Photochemistry and Photobiology B: Biology, 90, 187-197.
https://doi.org/10.1016/j.jphotobiol.2008.01.001

[10]   Sugio, S., Kashima, A., Mochizuki, S., Noda, M. and Kobayashi, K. (1999) Crystal Structure of Human Serum Albumin at 2.5 Angstrom Resolution. Protein Engineering, Design and Selection, 12, 439-446.
https://doi.org/10.1093/protein/12.6.439

[11]   Sudlow, G., Birkett, D.J. and Wade, D.N. (1975) Characterization of 2 Specific Drug Binding-Sites on Human Serum Albumin. Molecular Pharmacology, 11, 824-832.

[12]   Sudlow, G., Birkett, D.J. and Wade, D.N. (1976) Further Characterization of Specific Drug Binding Sites on Human Serum Albumin. Molecular Pharmacology, 12, 1052-1061.

[13]   Zhang, G., Wang, L. and Pan, J. (2012) Probing the Binding of the Flavonoid Diosmetin to Human Serum Albumin by Multispectroscopic Techniques. Journal of Agricultural and Food Chemistry, 60, 2721-2729.
https://doi.org/10.1021/jf205260g

[14]   Yue, Y., Liu, J., Liu, R., Sun, Y., Li, X. and Fan, J. (2014) The Binding Affinity of Phthalate Plasticizers-Protein Revealed by Spectroscopic Techniques and Molecular Modeling. Food and Chemical Toxicology, 71, 244-253.
https://doi.org/10.1016/j.fct.2014.06.022

[15]   Yue, Y., Liu, J., Fan, J. and Yao, X. (2011) Binding Studies of Phloridzin with Human Serum Albumin and Its Effect on the Conformation of Protein. Journal of Pharmaceutical and Biomedical Analysis, 56, 336-342.
https://doi.org/10.1016/j.jpba.2011.05.018

[16]   Sjoholm, I., Ekman, B., Kober, A., Ljungstedtpahlman, I., Seiving, B. and Sjodin, T. (1979) Binding of Drugs to Human-Serum Albumin:XI. Specificity of 3 Binding-Sites as Studied with Albumin Immobilized Microparticles. Molecular Pharmacology, 16, 767-777.

[17]   Park, H., Lee, J. and Lee, S. (2006) Critical Assessment of the Automated AutoDock as a New Docking Tool for Virtual Screening. Proteins: Structure Function and Bioinformatics, 65, 549-554.
https://doi.org/10.1002/prot.21183

[18]   Frisch, M.J. (2006) Optimizing Large Molecules with Gaussian 03. Chemicke Listy, 100, A9.

[19]   Feroz, S.R., Mohamad, S.B., Bujang, N., Malek, S.N.A. and Tayyab, S. (2012) Multispectroscopic and Molecular Modeling Approach to Investigate the Interaction of Flavokawain B with Human Serum Albumin. Journal of Agricultural and Food Chemistry, 60, 5899-5908.
https://doi.org/10.1021/jf301139h

[20]   Goddard, T.D., Huang, C.C. and Ferrin, T.E. (2007) Visualizing Density Maps with UCSF Chimera. Journal of Structural Biology, 157, 281-287.
https://doi.org/10.1016/j.jsb.2006.06.010

[21]   Eftink, M.R. and Ghiron, C.A. (1981) Fluorescence Quenching Studies with Proteins. Analytical Biochemistry, 114, 199-227.
https://doi.org/10.1016/0003-2697(81)90474-7

[22]   Albrecht, C., Joseph, R. and Lakowicz, J.R. (2008) Principles of Fluorescence Spectroscopy, 3rd Edition. Analytical and Bioanalytical Chemistry, 390, 1223-1224.
https://doi.org/10.1007/s00216-007-1822-x

[23]   Lakowicz, J.R. and Weber, G. (1973) Quenching of Fluorescence by Oxygen-Probe for Structural Fluctuations in Macromolecules. Biochemistry, 12, 4161-4170.
https://doi.org/10.1021/bi00745a020

[24]   Kathiravan, A., Chandramohan, M., Renganathan, R. and Sekar, S. (2009) Spectroscopic Studies on the Interaction between Phycocyanin and Bovine Serum Albumin. Journal of Molecular Structure, 919, 210-214.
https://doi.org/10.1016/j.molstruc.2008.09.005

[25]   Ware, W.R. (1962) Oxygen Quenching of Fluorescence in Solution: An Experimental Study of Diffusion Process. Journal of Physical Chemistry, 66, 455-458.
https://doi.org/10.1021/j100809a020

[26]   Gao, H., Lei, L.D., Liu, J.Q., Kong, Q., Chen, X.G. and Hu, Z.D. (2004) The Study on the Interaction between Human Serum Albumin and a New Reagent with Antitumour Activity by Spectrophotometric Methods. Journal of Photochemistry and Photobiology A: Chemistry, 167, 213-221.
https://doi.org/10.1016/j.jphotochem.2004.05.017

[27]   Suryawanshi, V.D., Anbhule, P.V., Gore, A.H., Patil, S.R. and Kolekar, G.B. (2012) Spectroscopic Investigation on the Interaction of Pyrimidine Derivative, 2-Amino- 6-Hydroxy-4-(3,4-Dimethoxyphenyl)-Pyrimidine-5-Carbonitrile with Human Serum Albumin: Mechanistic and Conformational Study. Industrial & Engineering Chemistry Research, 51, 95-102.
https://doi.org/10.1021/ie202005c

[28]   Makarska-Bialokoz, M. (2018) Comparative Study of Binding Interactions between Porphyrin Systems and Aromatic Compounds of Biological Importance by Multiple Spectroscopic Techniques: A Review. Spectrochimica Acta Part A: Molecular & Biomolecular Spectroscopy, 200, 263-274.
https://doi.org/10.1016/j.saa.2018.04.037

[29]   Makarskabialokoz, M. (2017) Interactions of Hemin with Bovine Serum Albumin and Human Hemoglobin: A Fluorescence Quenching Study. Spectrochimica Acta Part A: Molecular & Biomolecular Spectroscopy, 193, 23-32.
https://doi.org/10.1016/j.saa.2017.11.063

[30]   Hu, Y.-J., Ou-Yang, Y., Dai, C.-M., Liu, Y. and Xiao, X.-H. (2010) Site-Selective Binding of Human Serum Albumin by Palmatine: Spectroscopic Approach. Biomacromolecules, 11, 106-112.
https://doi.org/10.1021/bm900961e

[31]   Ross, P.D. and Subramanian, S. (1981) Thermodynamics of Protein Association Reactions: Forces Contributing to Stability. Biochemistry, 20, 3096-3102.
https://doi.org/10.1021/bi00514a017

[32]   Olsson, T.S.G., Williams, M.A., Pitt, W.R. and Ladbury, J.E. (2008) The Thermodynamics of Protein-Ligand Interaction and Solvation: Insights for Ligand Design. Journal of Molecular Biology, 384, 1002-1017.
https://doi.org/10.1016/j.jmb.2008.09.073

[33]   Tian, F.-F., Jiang, F.-L., Han, X.-L., Xiang, C., Ge, Y.-S., Li, J.-H., Zhang, Y., Li, R., Ding, X.-L. and Liu, Y. (2010) Synthesis of a Novel Hydrazone Derivative and Biophysical Studies of Its Interactions with Bovine Serum Albumin by Spectroscopic, Electrochemical, and Molecular Docking Methods. The Journal of Physical Chemistry B, 114, 14842-14853.
https://doi.org/10.1021/jp105766n

[34]   Ni, Y., Liu, Q. and Kokot, S. (2011) Spectrophotometric Study of the Interaction between Chlorotetracycline and Bovine Serum Albumin Using Eosin Y as Site Marker with the Aid of Chemometrics. Spectrochimica Acta Part A: Molecular & Biomolecular Spectroscopy, 78, 443-448.
https://doi.org/10.1016/j.saa.2010.11.007

[35]   Qi, Z.-D., Zhou, B., Xiao, Q., Shi, C., Liu, Y. and Dai, J. (2008) Interaction of Rofecoxib with Human Serum Albumin: Determination of Binding Constants and the Binding Site by Spectroscopic Methods. Journal of Photochemistry and Photobiology A: Chemistry, 193, 81-88.
https://doi.org/10.1016/j.jphotochem.2007.06.011

[36]   Forster, T. (1959) 10th Spiers Memorial Lecture. Transfer Mechanisms of Electronic Excitation. Discussions of the Faraday Society, 27, 7-17.
https://doi.org/10.1039/DF9592700007

[37]   Yue, Y., Chen, X., Qin, J. and Yao, X. (2009) Spectroscopic Investigation on the Binding of Antineoplastic Drug Oxaliplatin to Human Serum Albumin and Molecular Modeling. Colloids and Surfaces B: Biointerfaces, 69, 51-57.
https://doi.org/10.1016/j.colsurfb.2008.10.016

[38]   Schuphan, W. (1965) Biochemists Handbook. Qualitas Plantarum et Materiae Vegetabiles, 12, 218-230.

[39]   Valeur, B. and Berberan-Santos, M.N. (2012) Molecular Fluorescence: Principles and Applications. 2nd Edition, Wiley-VCH, Weinheim.
https://doi.org/10.1002/9783527650002

[40]   Zhou, J., Wu, X., Gu, X., Zhou, L., Song, K., Wei, S., Feng, Y. and Shen, J. (2009) Spectroscopic Studies on the Interaction of Hypocrellin A and Hemoglobin. Spectro-chimica Acta Part A: Molecular & Biomolecular Spectroscopy, 72, 151-155.
https://doi.org/10.1016/j.saa.2008.09.009

[41]   Mandal, P. and Ganguly, T. (2009) Fluorescence Spectroscopic Characterization of the Interaction of Human Adult Hemoglobin and Two Isatins, 1-Methylisatin and 1-Phenylisatin: A Comparative Study. The Journal of Physical Chemistry B, 113, 14904-14913.
https://doi.org/10.1021/jp9062115

[42]   Zaroog, M.S. and Tayyab, S. (2012) Formation of Molten Globule-Like State during Acid Denaturation of Aspergillus Niger Glucoamylase. Process Biochemistry, 47, 775-784.
https://doi.org/10.1016/j.procbio.2012.02.008

[43]   Zhang, J., Zhuang, S., Tong, C. and Liu, W. (2013) Probing the Molecular Interaction of Triazole Fungicides with Human Serum Albumin by Multispectroscopic Techniques and Molecular Modeling. Journal of Agricultural and Food Chemistry, 61, 7203-7211.
https://doi.org/10.1021/jf401095n

[44]   Wang, Y., Wang, X., Wang, J., Zhao, Y., He, W. and Guo, Z. (2011) Noncovalent Interactions between a Trinuclear Monofunctional Platinum Complex and Human Serum Albumin. Inorganic Chemistry, 50, 12661-12668.
https://doi.org/10.1021/ic201712e

 
 
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