Advanced search
Publication Cover
International Journal of Food Properties Volume 21, 2018 - Issue 1
Submit an article Journal homepage
1,304
Views
15
CrossRef citations to date
0
Altmetric
Articles

Conformation change of trypsin induced by acteoside as studied using multiple spectroscopic and molecular docking methods

Zhibing WuShenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, ChinaView further author information
,
Fengwen HuangShenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, ChinaView further author information
,
Yutao ChenShenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, China;School of Science, Faculty of Health and Environmental Sciences, Auckland University of Technology, Auckland, New ZealandView further author information
,
Hong XuShenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, China;Key Laboratory of RF Circuits and Systems of Ministry of Education, Hangzhou Dianzi University, Hangzhou, ChinaCorrespondence[email protected] [email protected]
View further author information
,
Manjunath D. MetiShenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, ChinaView further author information
,
Yu FanShenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, ChinaView further author information
,
Qingguo G. HanShenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, ChinaView further author information
,
Haifeng TangDepartment of Gynecology and Obstetrics, The University of Hong Kong-Shenzhen Hospital, Shenzhen, ChinaView further author information
,
Zhendan HeSchool of Medicine, Shenzhen University, Shenzhen, ChinaView further author information
&
Zhangli HuShenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, ChinaView further author information
 show all
Pages 301-312 | Received 05 Sep 2017, Accepted 16 Mar 2018, Published online: 20 Apr 2018

References

  • Lee, K. J.; Woo, E. R.; Choi, C. Y.; Shin, D. W.; Lee, D. G.; You, H. J.; Jeong, H. G. Protective Effect of Acteoside on Carbon Tetrachloride-Induced Hepatotoxicity. Life Sciences 2004, 74, 1051–1064. DOI: 10.1016/j.lfs.2003.07.020.
  • Xiong, Q.; Hase, K.; Tezuka, Y.; Namba, T.; Kadota, S. Acteoside Inhibits Apoptosis in D-Galactosamine and Lipopolysaccharide-Induced Liver Injury. Life Sciences 1999, 65, 421–430. DOI: 10.1016/S0024-3205(99)00263-5.
  • Arvizu-Flores, A. A.; Quintero-Reyes, I. E.; Felix-Lopez, M.; Islas-Osuna, M. A.; Yepiz-Plascencia, G.; Pacheco-Aguilar, R.; Navare, A.; Fernández, F. M.; Velazquez-Contreras, E. F.; Sotelo-Mundo, R. R.; et al. Thermodynamic Activation and Structural Analysis of Trypsin I from Monterey Sardine (Sardinops Sagax Caerulea). Food Chemistry 2012, 133, 898–904. DOI: 10.1016/j.foodchem.2012.01.111.
  • Ghosh, S.;. Interaction of Trypsin with Sodium Dodecyl Sulfate in Aqueous Medium: A Conformational View. Colloids and Surfaces B: Biointerfaces 2008, 66, 178–186. DOI: 10.1016/j.colsurfb.2008.06.011.
  • Stroud, R. M.; Kay, L. M.; Dickerson, R. E. The Structure of Bovine Trypsin: Electron Density Maps of the Inhibited Enzyme at 5 Å and at 2·7 Å Resolution. Journal of Molecular Biology 1974, 83, 185–208. DOI: 10.1016/0022-2836(74)90387-8.
  • Hörn, H.; Heidland, A. Proteases: Potential Role in Health and Diseases; Plenum Press: New York, 1992.
  • Reich, E.; Rifkin, D. B.; Shaw, E. Proteases and Biological Control; Cold Spring Harbor Laboratory: New York, 1975.
  • Liu, Y.; Zhang, G.; Zeng, N.; Hu, S. Interaction between 8-Methoxypsoralen and Trypsin: Monitoring by Spectroscopic, Chemometrics and Molecular Docking Approaches. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2017, 173, 188–195. DOI: 10.1016/j.saa.2016.09.015.
  • Li, Q.; Wei, Q.; Yuan, E.; Yang, J.; Ning, Z. Interaction between Four Flavonoids and Trypsin: Effect on the Characteristics of Trypsin and Antioxidant Activity of Flavonoids. International Journal of Food Science and Technology 2014, 49, 1063–1069. DOI: 10.1111/ijfs.12401.
  • Shen, L.; Xu, H.; Huang, F.; Li, Y.; Xiao, H.; Yang, Z.; Hu, Z.; He, Z.; Zeng, Z.; Li, Y. Investigation on Interaction between Ligupurpuroside A and Pepsin by Spectroscopic and Docking Methods. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2015, 135, 256–263. DOI: 10.1016/j.saa.2014.06.087.
  • Wang, J.; Chan, C.; Huang, F. W.; Xie, J. F.; Xu, H.; Ho, K. W.; Zheng, S. G.; Hu, Z. L.; Lu, J.; He, Z. D. Interaction Mechanism of Pepsin with a Natural Inhibitor Gastrodin Studied by Spectroscopic Methods and Molecular Docking. Medicinal Chemistry Research 2017, 26, 405–413. DOI: 10.1007/s00044-016-1760-2.
  • Ying, M.; Huang, F.; Ye, H.; Xu, H.; Shen, L.; Huan, T.; Huang, S.; Xie, J.; Tian, S.; Hu, Z.; et al. Study on Interaction between Curcumin and Pepsin by Spectroscopic and Docking Methods. International Journal of Biological Macromolecules 2015, 79, 201–208. DOI: 10.1016/j.ijbiomac.2015.04.057.
  • Fang, Y.; Xu, H.; Shen, L.; Huang, F.; Yibulayin, S.; Huang, S.; Tian, S.; Hu, Z.; He, Z.; Li, F.; et al. Study on the Mechanism of the Interaction between Acteoside and Pepsin Using Spectroscopic Techniques. Luminescence. 2015, 30, 859–866. DOI: 10.1002/bio.v30.6.
  • Xu, H.; Zhu, Q. Q.; Lu, J.; Chen, X. J.; Xiao, J.; Liu, Z. G.; Chen, S. P.; Tong, M. L.; Ji, L. N.; Liang, Y. Studies on Thermodynamic Nature of Steroselectivity for Ruthenium (II) Polypyridyl Complex Binding to DNA. Inorganic Chemistry Communications 2010, 13, 711–714. DOI: 10.1016/j.inoche.2010.03.025.
  • Wu, Z.; Shen, L.; Han, Q.; Lu, J.; Tang, H.; Xu, X.; Xu, H.; Huang, F.; Xie, J.; He, Z.; et al. Mechanism and Nature of Inhibition of Trypsin by Ligupurpuroside A, a Ku-Ding Tea Extract, Studied by Spectroscopic and Docking Methods. Food Biophysics 2017, 12, 78–87. DOI: 10.1007/s11483-016-9465-0.
  • Hong, W. X.; Huang, F.; Huan, T.; Xu, X.; Han, Q.; Wang, G.; Xu, H.; Duan, S.; Duan, Y.; Long, X.; et al. Comparative Studies on DNA-binding and in Vitro Antitumor Activity of Enantiomeric Ruthenium (II) Complexes. Journal of Inorganic Biochemistry 2018, 180, 54–60. DOI: 10.1016/j.jinorgbio.2017.11.024.
  • Wong, I. Y. F.; He, Z. D.; Huang, Y.; Chen, Z. Y. Antioxidative Activities of Phenylethanoid Glycosides from Ligustrum Purpurascens. Journal of Agricultural and Food Chemistry 2001, 49, 3113–3119. DOI: 10.1021/jf0100604.
  • Song, W.; Yu, Z.; Hu, X.; Liu, R. Dissection of the Binding of Hydrogen Peroxide to Trypsin Using Spectroscopic Methods and Molecular Modeling. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2015, 137, 286–293. DOI: 10.1016/j.saa.2014.08.037.
  • Gholami, S.; Bordbar, A. K. Exploring Binding Properties of Naringenin with Bovine β-lactoglobulin: A Fluorescence, Molecular Docking and Molecular Dynamics Simulation Study. Biophysical Chemistry 2014, 187-188, 33–42. DOI: 10.1016/j.bpc.2014.01.003.
  • GonçAlves, R.; Mateus, N.; De Freitas, V. Biological Relevance of the Interaction between Procyanidins and Trypsin: A Multitechnique Approach. Journal of Agricultural and Food Chemistry 2010, 58, 11924–11931. DOI: 10.1021/jf1023356.
  • Mandal, P.; Ganguly, T. 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 2009, 113, 14904–14913. DOI: 10.1021/jp9062115.
  • Bhomia, R.; Trivedi, V.; Coleman, N. J.; Mitchell, J. C. The Thermal and Storage Stability of Bovine Haemoglobin by Ultraviolet-Visible and Circular Dichroism Spectroscopies. Journal of Pharmaceutical Analysis 2016, 6, 242–248. DOI: 10.1016/j.jpha.2016.02.004.
  • Chi, Z.; Liu, R.; Zhang, H. Noncovalent Interaction of Oxytetracycline with the Enzyme Trypsin. Biomacromolecules. 2010, 11, 2454–2459. DOI: 10.1021/bm100633h.
  • Hu, X.; Yu, Z.; Liu, R. Spectroscopic Investigations on the Interactions between Isopropanol and Trypsin at Molecular Level. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2013, 108, 50–54. DOI: 10.1016/j.saa.2013.01.072.
  • Yu, X.; Yang, Y.; Zou, X.; Tao, H.; Ling, Y.; Yao, Q.; Zhou, H.; Yi, P. Study on the Interaction between Novel Spiro Pyrrolidine and Bovine Serum Albumin by Spectroscopic Techniques. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2012, 94, 23–29. DOI: 10.1016/j.saa.2012.03.050.
  • Wang, Y. Q.; Tan, C. Y.; Zhuang, S. L.; Zhai, P. Z.; Cui, Y.; Zhou, Q. H.; Zhang, H. M.; Fei, Z. In Vitro and in Silico Investigations of the Binding Interactions between Chlorophenols and Trypsin. Journal of Hazardous Materials 2014, 278, 55–65. DOI: 10.1016/j.jhazmat.2014.05.092.
  • Wang, Q.; Huang, C. R.; Jiang, M.; Zhu, Y. Y.; Wang, J.; Chen, J.; Shi, J. H. Binding Interaction of Atorvastatin with Bovine Serum Albumin: Spectroscopic Methods and Molecular Docking. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2016, 156, 155–163. DOI: 10.1016/j.saa.2015.12.003.
  • Sahoo, B. K.; Ghosh, K. S.; Dasgupta, S. Molecular Interactions of Isoxazolcurcumin with Human Serum Albumin: Spectroscopic and Molecular Modeling Studies. Biopolymers. 2009, 91, 108–119. DOI: 10.1002/bip.v91:2.
  • Abou-Zied, O. K.; Al-Shihi, O. I. K. Characterization of Subdomain IIA Binding Site of Human Serum Albumin in Its Native, Unfolded, and Refolded States Using Small Molecular Probes. Journal of the American Chemical Society 2008, 130, 10793–10801. DOI: 10.1021/ja8031289.
  • Bozoğlan, B. K.; Tunç, S.; Duman, O. Investigation of Neohesperidin Dihydrochalcone Binding to Human Serum Albumin by Spectroscopic Methods. Journal of Luminescence 2014, 155, 198–204. DOI: 10.1016/j.jlumin.2014.06.032.
  • Cui, F.; Yan, Y.; Zhang, Q.; Yao, X.; Qu, G.; Lu, Y. Characterization of the Interaction between 8-Bromoadenosine with Human Serum Albumin and Its Analytical Application. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2009, 74, 964–971. DOI: 10.1016/j.saa.2009.09.001.
  • Shu, Y.; Xue, W.; Xu, X.; Jia, Z.; Yao, X.; Liu, S.; Liu, L. Interaction of Erucic Acid with Bovine Serum Albumin Using a Multi-Spectroscopic Method and Molecular Docking Technique. Food chemistry 2015, 173, 31–37. DOI: 10.1016/j.foodchem.2014.09.164.
  • Sarkar, M.; Paul, S. S.; Mukherjea, K. K. Interaction of Bovine Serum Albumin with a Psychotropic Drug Alprazolam: Physicochemical, Photophysical and Molecular Docking Studies. Journal of Luminescence 2013, 142, 220–230. DOI: 10.1016/j.jlumin.2013.03.026.
  • Sharma, A. S.; Anandakumar, S.; Ilanchelian, M. A Combined Spectroscopic and Molecular Docking Study on Site Selective Binding Interaction of Toluidine Blue O with Human and Bovine Serum Albumins. Journal of Luminescence 2014, 151, 206–218. DOI: 10.1016/j.jlumin.2014.02.009.
  • Jayabharathi, J.; Jayamoorthy, K.; Thanikachalam, V. Docking Investigation and Binding Interaction of Benzimidazole Derivative with Bovine Serum Albumin. Journal of Photochemistry and Photobiology B: Biology 2012, 117, 27–32. DOI: 10.1016/j.jphotobiol.2012.08.018.
  • Wang, J.; Liu, R.; Qin, P. Toxic Interaction between Acid Yellow 23 and Trypsin: Spectroscopic Methods Coupled with Molecular Docking. Journal of Biochemical and Molecular Toxicology 2012, 26, 360–367. DOI: 10.1002/jbt.v26.9.
  • Wang, Y.; Zhang, G.; Wang, L. Potential Toxicity of Phthalic Acid Esters Plasticizer: Interaction of Dimethyl Phthalate with Trypsin in Vitro. Journal of Agricultural and Food Chemistry 2014, 63, 75–84. DOI: 10.1021/jf5046359.
  • Simon, L. M.; Kotorman, M.; Garab, G.; Laczko, I. Structure and Activity of α-Chymotrypsin and Trypsin in Aqueous Organic Media. Biochemical and Biophysical Research Communications 2001, 280, 1367–1371. DOI: 10.1006/bbrc.2001.4282.
  • Wu, X.; He, W.; Wang, W.; Luo, X.; Cao, H.; Lin, L.; Feng, K.; Liu, Z. Investigation of the Interaction between (−)-Epigallocatechin-3-Gallate with Trypsin and α-chymotrypsin. International Journal of Food Science and Technology 2013, 48, 2340–2347.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.