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Research Article

Dissection of binding of trypsin to its natural inhibitor Gensenoside-Rg1 using spectroscopic methods and molecular modeling

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Pages 4070-4079 | Received 26 Jul 2018, Accepted 17 Oct 2018, Published online: 18 Nov 2018

References

  • Bijari, N., Shokoohinia, Y., Ashrafi-Kooshk, M. R., Ranjbar, S., Parvaneh, S., Moieni-Arya, M., & Khodarahmi, R. (2013). Spectroscopic study of interaction between osthole and human serum albumin: Identification of possible binding site of the compound. Journal of Luminescence, 143(6), 328–336. doi:10.1016/j.jlumin.2013.04.045
  • Chen, T.-T., Zhu, X.-T., Chen, Q., Ge, M., Jia, X.-P., Wang, X., & Ge, C.-W. (2015). Interaction between Z-ligustilide from Radix Angelica sinensis and human serum albumin. Food Chemistry, 186, 292–297. doi:10.1016/j.foodchem.2014.11.041
  • Cui, F.-L., Zhang, Q.-Z., Yan, Y.-H., Yao, X.-J., Qu, G.-R., & Lu, Y. (2008). Study of characterization and application on the binding between 5-iodouridine with HSA by spectroscopic and modeling. Carbohydrate Polymers, 73(3), 464–472. doi:10.1016/j.carbpol.2007.12.032
  • Fan, Y., Xu, Y., Han, Q.-G., Shen, L.-L., Xu, H., Wu, Z.-B., … Hu, Z.-L. (2018). Exploring inhibition mechanism and nature of lipase by Ligupurpuroside A extracted from Ku-Ding tea. Medicinal Chemistry Research, 27(7), 1822–1833. doi:10.1007/s00044-018-2194-9
  • Fang, Y., Xu, H., Shen, L., Huang, F., Yibulayin, S., Huang, S., … Zhou, K. (2015). Study on the mechanism of the interaction between acteoside and pepsin using spectroscopic techniques. Luminescence, 30(6), 859–866. doi:10.1002/bio.2833
  • Gao, Y., Zi, Y.-Q., Shao, C.-Y., & Wang, M.-R. (2014). Analysis of binding interaction between vitamin B2 and trypsin. Research on Chemical Intermediates, 40(8), 3135–3144. doi:10.1007/s11164-013-1159-3
  • Gökoğlu, E., Yılmaz, E., Gökoğlu, E., & Baran, A. U. (2016). Study of binding properties between two new ibuprofen and naproxen based acyl hydrazone derivatives and trypsin. Journal of Fluorescence, 26(1), 113–119. doi:10.1007/s10895-015-1690-2
  • GonçAlves, R., Mateus, N., &., & De Freitas, V. (2010). Biological relevance of the interaction between procyanidins and trypsin: A multitechnique approach. Journal of Agricultural and Food Chemistry, 58(22), 11924–11931. doi:10.1021/jf1023356
  • He, W., Dou, H.-J., Zhang, L., Wang, L.-J., Wang, R.-Y., & Chang, J.-B. (2014). Spectroscopic study on the interaction of trypsin with bicyclol and analogs. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 118, 510–519. doi:10.1016/j.saa.2013.09.027
  • Hong, W.-X., Huang, F., Huan, T., Xu, X., Han, Q., Wang, G., … Hu, Z. (2018). Comparative studies on DNA-binding and in vitro antitumor activity of enantiomeric ruthenium (II) complexes. Journal of Inorganic Biochemistry, 180, 54–60. doi:10.1016/j.jinorgbio.2017.11.024
  • Hu, X.-X., Yu, Z.-H., & Liu, R.-T. (2013). Spectroscopic investigations on the interactions between isopropanol and trypsin at molecular level. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 108, 50–54. doi:10.1016/j.saa.2013.01.072
  • Hu, Y.-J., Liu, Y., Zhang, L.-X., Zhao, R.-M., & Qu, S.-S. (2005). Studies of interaction between colchicine and bovine serum albumin by fluorescence quenching method. Journal of Molecular Structure, 750(1–3), 174–178. doi:10.1016/j.molstruc.2005.04.032
  • Huang, Y.-B., Yan, J., Liu, B.-Z., Yu, Z., Gao, X.-Y., Tang, Y.-C., & Zi, Y.-Q. (2010). Investigation on interaction of prulifloxacin with pepsin: A spectroscopic analysis. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 75(3), 1024–1029. doi:10.1016/j.saa.2009.12.044
  • Huang, Y.-M., Wang, Q., Yang, H.-Q., Tang, B., Ma, X.-L., He, J.-W., & Li, H. (2017). Probing the binding of Azilsartan to DNA by molecular docking, steady-state/time-resolved fluorescence, viscosity, infrared, and circular dichroism spectra. Spectroscopy Letters, 50(1), 39–47. doi:10.1080/00387010.2017.1282526
  • Kandagal, P. B., Ashoka, S., Seetharamappa, J., Shaikh, S. M. T., Jadegoud, Y., & Ijare, O. B., (2006). Study of the interaction of an anticancer drug with human and bovine serum albumin: spectroscopic approach. Journal of Pharmaceutical and Biomedical Analysis, 41(2), 393–399. doi:10.1016/j.jpb. a.2005.11.037
  • Koutsopoulos, S., Patzsch, K., Bosker, W. T., & Norde, W. (2007). Adsorption of trypsin on hydrophilic and hydrophobic surfaces. Langmuir, 23(4), 2000–2006. doi:10.1021/la062238s
  • Lakowicz, J. R., & Weber, G. (1973). Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules. Biochemistry, 12(21), 4161–4170. doi:10.1021/bi00745a020
  • Laskowski, R. A., & Swindells, M. B. (2011). LigPlot+: Multiple ligand–protein interaction diagrams for drug discovery. Journal of Chemical Information and Modeling, 51(10), 2778–2786. doi:10.1021/ci200227u
  • Lee, Y., Jin, Y., Lim, W., Ji, S., Choi, S., Jang, S., & Lee, S. (2003). A ginsenoside-Rh1, a component of ginseng saponin, activates estrogen receptor in human breast carcinoma MCF-7 cells. Journal of Steroid Biochemistry and Molecular Biology, 84(4), 463–468. doi:10.1016/S0960-0760(03)00067-0
  • Li, H., Pu, J.-J., Wang, Y., Liu, C., Yu, J., Li, T., & Wang, R.-Q. (2013). Comparative study of the binding of Trypsin with bifendate and analogs by spectrofluorimetry. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 115, 1–11. doi:10.1016/j.saa.2013.06.025
  • Li, X., Li, M., Li, Y., Quan, Q.-K., & Wang, J. (2012). Cellular and molecular mechanisms underlying the action of ginsenoside Rg1 against Alzheimer’s disease. Neural Regeneration Research, 7(36), 2860–2866. doi:10.3969/j.issn.1673-5374.2012.36.002
  • Liu, J.-M., Yan, X.-Y., Yue, Y.-Y., & Zhao, S.-F. (2018). Investigation of the interaction of aurantio‐obtusin with human serum albumin by spectroscopic and molecular docking methods. Luminescence, 33(1), 104–111. doi:10.1002/bio.3378
  • Liu, J.-M., Yue, Y.-Y., Wang, J., Yan, X.-Y., Liu, R., Sun, Y.-Y., & Li, X.-G. (2015). Study of interaction between human serum albumin and three phenanthridine derivatives: Fluorescence spectroscopy and computational approach. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 145, 473–481. doi:10.1016/j.saa.2015.03.069
  • Lou, Y.-Y., Zhou, K.-L., Pan, D. Q., Shen, J.-L., & Shi, J.-H. (2017). Spectroscopic and molecular docking approaches for investigating conformation and binding characteristics of clonazepam with bovine serum albumin (BSA). Journal of Photochemistry and Photobiology B: Biology, 167, 158–167. doi:10.1016/j.jphotobiol.2016.12.029
  • Lu, Y., Wang, G.-K., Lu, X.-M., Lv, J., Xu, M.-H., & Zhang, W.-W. (2010). Molecular mechanism of interaction between norfloxacin and trypsin studied by molecular spectroscopy and modeling. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 75(1), 261–266. doi: 10.1016/j.saa.2009.10.021
  • Luo, X., Du, C.-R., Wei, J.-R., Deng, J., Lin, Y.-J., & Lin, C.-W. (2013). Study of the interaction between sodium salts of (2E)-3-(4′-halophenyl) prop-2-enoyl sulfachloropyrazine and bovine serum albumin by fluorescence spectroscopy. Luminescence, 28(2), 202–210. doi:10.1002/bio.2364
  • Mariam, J., Dongre, P. M., & Kothari, D. C. (2011). Study of interaction of silver nanoparticles with bovine serum albumin using fluorescence spectroscopy. Journal of Fluorescence, 21(6), 2193–2199. doi:10.1007/s10895-011-0922-3
  • Meti, M. D., Lin, J., Wang, Y., Wu, Z., Xu, H., Xu, X., … He, Z. (2018). Trypsin inhibition by Ligupurpuroside B as studied using spectroscopic, CD and molecular docking techniques. Journal of Biomolecular Structure & Dynamics, 36, 1–31. doi:10.1080/07391102.2018.1515115
  • Meti, M. D., Xu, Y., Xie, J.-F., Chen, Y.-T., Wu, Z.-B., Liu, J., … Xu, H. (2018b). Multi-spectroscopic studies on the interaction between traditional Chinese herb, helicid with pepsin. Molecular Biology Reports, 36, 1–10. doi:10.1007/s11033-018-4306-5
  • Nguyen, T. D., Moody, M. W., Steinhoff, M., Okolo, C., Koh, D. S., & Bunnett, N. W. (1999). Trypsin activates pancreatic duct epithelial cell ion channels through proteinase-activated receptor-2. Journal of Clinical Investigation, 103(2), 261–269. doi:10.1172/JCI2539
  • Ross, P. D., & Subramanian, S. (1981). Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry, 20(11), 3096–3102. doi:10.1021/bi00514a017
  • Shahlaei, M., Rahimi, B., Nowroozi, A., Ashrafi-Kooshk, M. R., Sadrjavadi, K., & Khodarahmi, R. (2015). Exploring binding properties of sertraline with human serum albumin: Combination of spectroscopic and molecular modeling studies. Chemico-Biological Interactions, 242, 235–246. doi: 10.1016/j.cbi.2015.10.006
  • Shen, L., Xu, H., Huang, F., Li, Y., Xiao, H., Yang, Z., … Li, Y. (2015). Investigation on interaction between Ligupurpuroside A and pepsin by spectroscopic and docking methods. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 135, 256–263. doi:10.1016/j.saa.2014.06.087
  • Shuai, L., Chen, Z., Fei, P., Wang, Q., & Yang, T.-M. (2014). Spectroscopic analysis on the interaction of ferulic acid and tetramethylpyrazine with trypsin. Luminescence, 29(1), 79–86. doi:10.1002/bio.2506
  • Song, W., Yu, Z.-H., Hu, X.-X., & Liu, R.-T. (2015). Dissection of the binding of hydrogen peroxide to trypsin using spectroscopic methods and molecular modeling. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 137, 286–293. doi:10.1016/j.saa.2014.08.037
  • Song, X.-Y., Hu, J.-F., Chu, S.-F., Zhang, Z., Xu, S., Yuan, Y.-H., … Chen, N.-H. (2013). Ginsenoside Rg1 attenuates okadaic acid induced spatial memory impairment by the GSK3β/tau signaling pathway and the Aβ formation prevention in rats. European Journal of Pharmacology, 710(1–3), 29–38. doi:10.1016/j.ejphar.2013.03.051
  • Sreerama, N., & Woody, R. W. (2004). Computation and analysis of protein circular dichroism spectra. Methods Enzymology, 383, 318–351. doi:10.1016/S0076-6879(04)83013-1
  • Sun, H.-W., Wu, Y.-J., Xia, X.-H., & Shi, Z.-H. (2013). Spectroscopic studies on the interaction characteristics between norethisterone and bovine serum albumin. Journal of Luminescence, 134, 580–587. doi:10.1016/j.jlumin.2012.07.026
  • Wang, C.-X., Yan, F.-F., Zhang, Y.-X., & Ye, L. (2007). Spectroscopic investigation of the interaction between rifabutin and bovine serum albumin. Journal of Photochemistry and Photobiology A: Chemistry, 192(1), 23–28. doi:10.1016/j.jphotochem.2007.04.032
  • Wang, J., Chan, C., Huang, F-W., Xie, J-F., Xu, H., Ho, K-W., … He, Z-D. (2017). Interaction mechanism of pepsin with a natural inhibitor gastrodin studied by spectroscopic methods and molecular docking. Medicinal Chemistry Research, 26(2), 405–413. doi:10.1007/s00044-016-1760-2
  • Wang, Y.-P., Wei, Y.-L., & Dong, C. (2006). Study on the interaction of 3, 3-bis (4-hydroxy-1-naphthyl)-phthalide with bovine serum albumin by fluorescence spectroscopy. Journal of Photochemistry and Photobiology A: Chemistry, 117, 177(1), 6–11. doi:10.1016/j.jphotochem.2005.04.040
  • Wang, Y.-P., Zhang, G.-W., & Wang, L.-H. (2014). Interaction of prometryn to human serum albumin: Insights from spectroscopic and molecular docking studies. Pesticide Biochemistry and Physiology, 108, 66–73. doi:10.1016/j.pestbp.2013.12.006
  • Wang, Y.-P., Zhang, G.-W., & Wang, L.-H. (2015). Potential toxicity of phthalic acid esters plasticizer: Interaction of dimethyl phthalate with trypsin in vitro. Journal of Agricultural and Food Chemistry, 63(1), 75–84. doi:10.1021/jf5046359
  • Wang, Y.-Q., Chen, T.-T., & Zhang, H.-M. (2010). Investigation of the interactions of lysozyme and trypsin with biphenol A using spectroscopic methods. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 75(3), 1130–1137. doi:10.1016/j.saa.2009.12.071
  • Wang, Y.-Q., Zhang, H.-M., Cao, J., & Zhou, Q.-H. (2013). Interaction of methotrexate with trypsin analyzed by spectroscopic and molecular modeling methods. Journal of Molecular Structure, 1051, 78–85. doi:10.1016/j.molstruc.2013.07.048
  • Wang, Y.-Q., Zhang, H.-M., Zhang, G.-C., Liu, S.-X., Zhou, Q.-H., Fei, Z.-H., & Liu, Z.-T. (2007). Studies of the interaction between paraquat and bovine hemoglobin. International Journal of Biological Macromolecules, 41(3), 243–250. doi:10.1016/j.ijbiomac.2007.02.011
  • Wu, Z., Shen, L., Han, Q., Lu, J., Tang, H., Xu, X., … Hu, Z. (2017). Mechanism and nature of inhibition of trypsin by Ligupurpuroside A, a Ku-Ding tea extract, studied by spectroscopic and docking methods. Food Biophysics, 12(1), 78–87. doi:10.1007/s11483-016-9465-0
  • Wu, Z., Huang, F., Chen, Y., Xu, H., Meti, M. D., Fan, Y., … Hu, Z. (2018). Conformation change of trypsin induced by acteoside as studied using multiple spectroscopic and molecular docking methods. International Journal of Food Properties, 21(1), 301–312. doi:10.1080/10942912.2018.1454944
  • Xie, C.-L., Wang, W.-W., Xue, X.-D., Zhang, S.-F., Gan, J., & Liu, Z.-G. (2015). A systematic review and meta-analysis of Ginsenoside-Rg1 (G-Rg1) in experimental ischemic stroke. Scientific Reports, 5, 7790. doi:10.1038/srep07790
  • Xu, H., Zhu, Q.-Q., Lu, J., Chen, X.-J., Xiao, J., Liu, Z.-G., … Liang, Y. (2010). Studies on thermodynamic nature of stereoselectivity for ruthenium (II) polypyridyl complex binding to DNA. Inorganic Chemistry Communication, 13(6), 711–714. doi:10.1016/j.inoche.2010.03.025
  • Ying, M., Huang, F., Ye, H., Xu, H., Shen, L., Huan, T., … Zhou, K. (2015). Study on interaction between curcumin and pepsin by spectroscopic and docking methods. International Journal of Biological Macromolecules, 79, 201–208. doi:10.1016/j.ijbiomac.2015.04.057
  • Ying, M., Meti, M. D., Xu, H., Wang, Y., Lin, J., Wu, Z., … Hu, Z. (2018). Binding mechanism of lipase to Ligupurpuroside B extracted from Ku-Ding tea as studied by multi-spectroscopic and molecular docking methods. International Journal of Biological Macromolecules, 120, 1345–1352. doi:10.1016/j.ijbiomac.2018.09.086
  • Yue, Y.-Y., Dong, Q., Zhang, Y.-J., Li, X.-G., Yan, X.-Y., Sun, Y.-H., & Liu, J.-M. (2016a). Synthesis of imidazole derivatives and the spectral characterization of the binding properties towards human serum albumin. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 153, 688–703. doi:10.1016/j.saa.2015.09.023
  • Yue, Y.-Y., Sun, Y.-Y., Dong, Q., Liu, R., Yan, X.-Y., Zhang, Y.-J., & Liu, J.-M. (2016b). Interaction of human serum albumin with novel imidazole derivatives studied by spectroscopy and molecular docking. Luminescence, 31(3), 671–681. doi:10.1002/bio.3010
  • Yue, Y.-Y., Sun, Y.-Y., Yan, X.-Y., Liu, J.-M., Zhao, S.-F., & Zhang, J. (2016c). Evaluation of the binding of perfluorinated compound to pepsin: Spectroscopic analysis and molecular docking. Chemosphere, 161, 475–481. doi:10.1016/j.chemosphere.2016.07.047
  • Yue, Y.-Y., Wang, Z.-Y., Wang, Z.-X., Zhang, Y.-Y., & Liu, J.-M. (2018). A comparative study of binding properties of different coumarin-based compounds with human serum albumin. Journal of Molecular Structure, 1169, 75–80. doi:10.1016/j.molstruc.2018.05.060
  • Yue, Y.-Y., Zhao, S.-F., Liu, J.-M., Yan, X.-Y., & Sun, Y.-Y. (2017a). Probing the binding properties of dicyandiamide with pepsin by spectroscopy and docking methods. Chemosphere, 185, 1056–1062. doi:10.1016/j.chemosphere.2017.07.115
  • Yue, Y.-Y., Zhao, S.-F., Sun, Y.-Y., Yan, X.-Y., Liu, J.-M., & Zhang, J. (2017b). Effects of plant extract aurantio-obtusin on pepsin structure: Spectroscopic characterization and docking simulation. Journal of Luminescence, 187, 333–339. doi:10.1016/j.jlumin.2017.03.041
  • Zeng, H.-J., You, J., Liang, H.-L., Qi, T.-T., Yang, R., & Qu, L.-B. (2014). Investigation on the binding interaction between silybin and pepsin by spectral and molecular docking. International Journal of Biological Macromolecules, 67, 105–111. doi:10.1016/j.ijbiomac.2014.02.051

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