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Effects of Forsythoside E on Acetylcholinesterase and Butyrylcholinesterase by Fluorescent Spectroscopy

Abstract

Forsythoside E is one of the major secondary metabolites in Forsythia suspensa. The interactions between forsythoside E and two types of cholinesterases, acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) were investigated in PBS buffer (pH 7.40) by using multispectroscopic techniques. Forsythoside E increased the fluorescence intensity of AChE but quenched the fluorescence of BChE. Synchronous fluorescence studies showed that forsythoside E mainly acts on tyrosine residues of AChE and tryptophan residues of BChE. It was also proved that the complex between the compound and cholinesterases formed spontaneously at a stoichiometric ratio of 1:1 via multispectral technology. Finally, forsythoside E inhibited the activities of cholinesterases with similar IC50 values of 1.08 mM for AChE and 0.92 mM for BChE. The results illuminate the details of the interaction between forsythoside E and cholinesterases.

About the Authors

Ch. Gao
Institute of Molecular Science at Shanxi University
China

Taiyuan



H. Du
Institute of Molecular Science at Shanxi University
China

Taiyuan



References

1. T. H. Ferreira-Vieira, I. M. Guimaraes, F. R. Silva, F. M. Ribeiro, Curr. Neuropharmacol., 14, 101 (2016).

2. H. Hampel, M. M. Mesulam, A. C. Cuello, A. S. Khachaturian, A. Vergallo, M. R. Farlow, P. J. Snyder, E. Giacobini, Z. S. Khachaturian, J. Prev. Alzheimers Dis., 6, 2 (2019).

3. S. S. Xing, Q. Li, B. C. Xiong, Y. Chen, F. Feng, W. Y. Liu, H. P. Sun, Med. Res. Rev., 41, 858 (2020).

4. H. Dvir, I. Silman, M. Harel, T.L. Rosenberry, J. L. Sussman, Chem. Biol. Interact., 187, 10 (2010).

5. N. C. Inestrosa, A. Alvarez, C. A. Pérez, R. D. Moreno, M. Vicente, C. Linker, O. I. Casanueva, C. Soto, J. Garrido, Neuron, 16, 881 (1996).

6. M. Mehta, A. Adem, M. Sabbagh, Int. J. Alzheimers Dis., 2012, 728983 (2012).

7. B. Adalat, F. Rahim, M. Taha, F. J. Alshamrani, E. H. Anouar, N. Uddin, S. A. A. Shah, Z. Ali, Z. A. Zakaria, Molecules, 25, 4828 (2020).

8. P. Anand, B. Singh, Arch. Pharm. Res., 36, 375 (2013).

9. [CPH] Chinese Pharmacopoeia Commission, Pharmacopoeia of the People’s Republic of China. Part Five, China Medical Science Press, 170 (2020).

10. F. N. Wang, Z. Q. Ma, Y. Liu, Y. Z. Guo, Z. W. Gu, Molecules, 14, 1324 (2009).

11. Y. Li, Q. Guo, Y. Yan, T. Chen, C. Du, H. Du, Spectrochim. Acta A: Mol. Biomol. Spectrosc., 214, 309 (2019).

12. X. Yan, T. Chen, L. Zhang, H. Du, Eur. J. Pharmacol., 810, 141 (2017).

13. X. Yan, T. Chen, L. Zhang, H. Du, Int. J. Biol. Macromol., 119, 1344 (2018).

14. M. Georgiev, K. Alipieva, I. Orhan, R. Abrashev, P. Denev, M. Angelova, Food Chem., 128, 100 (2011).

15. B. Ahmad, S. Parveen, R. H. Khan, Biomacromolecules, 7, 1350 (2006).

16. G. L. Ellman, K. D. Courtney, V. Andres, R. M. Featherstone, Biochem. Pharmacol., 7, 88 (1961).

17. R. Li, D. Dhankhar, J. Chen, T. C. Cesario, P. M. Rentzepis, Proc. Natl. Acad. Sci. USA, 116, 18822 (2019).

18. J. N. Miller, Proc. Anal. Div. Chem. Soc., 16, 203 (1979).

19. P. D. Ross, S. Subramanian, Biochemistry, 20, 3096 (1981).

20. U. Anand, C. Jash, S. Mukherjee, J. Phys. Chem. B, 114, 15839 (2010).

21. J. R. Lackowicz, Principles of Fluorescence Spectroscopy, 3rd ed., Plenum Press, New York, 603–606 (2006).

22. S. Nusrat, A. Masroor, M. Zaman, M. K. Siddiqi, M. R. Ajmal, N. Zaidi, A. S. Abdelhameed, R. H. Khan, Int. J. Biol. Macromol., 109, 1132 (2018).

23. I. M. Klotz, Ann. N. Y. Acad. Sci., 226, 18 (1973).

24. D. Leckband, Annu. Rev. Biophys. Biomol. Struct., 29, 1 (2000).


Review

For citations:


Gao Ch., Du H. Effects of Forsythoside E on Acetylcholinesterase and Butyrylcholinesterase by Fluorescent Spectroscopy. Zhurnal Prikladnoii Spektroskopii. 2022;89(3):432.

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ISSN 0514-7506 (Print)