zhpsЖурнал прикладной спектроскопииZhurnal Prikladnoii Spektroskopii0514-7506B. I. Stepanov Institute of Physics of the National Academy of Scienceszhps-1068Research ArticleАННОТАЦИИ АНГЛОЯЗЫЧНЫХ СТАТЕЙABSTRACTS ENGLISH-LANGUAGE ARTICLESВлияние форситозида E на ацетилхолинэстеразу и бутирилхолинэстеразу по данным флуоресцентной спектроскопииEffects of Forsythoside E on Acetylcholinesterase and Butyrylcholinesterase by Fluorescent SpectroscopyGaoCh.GaoCh.

Тайюань

Taiyuan

DuH.DuH.

Тайюань

Taiyuan

duhuizhi@sxu.edu.cnИнститут молекулярных наук Шаньсийского университетаInstitute of Molecular Science at Shanxi University202226052022893432432Copyright © Gao C., Du H., 20222022Gao C., Du H.Gao C., Du H.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://zhps.ejournal.by/jour/article/view/1068

Исследовано взаимодействие между одним из основных вторичных метаболитов Forsythia suspensa форcитозидом Е и двумя типами холинэстераз — ацетилхолинэстеразой (АХЭ) и бутирилхолинэстеразой (БХЭ) — в буфере PBS (рН 7.40) с использованием спектроскопических методов. Показано, что форcитозид Е увеличивает интенсивность флуоресценции АХЭ, но подавляет флуоресценцию БХЭ, при этом воздействует преимущественно на тирозиновые остатки АХЭ и триптофановые остатки БХЭ. Доказано, что комплекс между форcитозидом Е и холинэстеразами образуется спонтанно при стехиометрическом соотношении 1:1 и форситозид Е ингибирует активность холинэстераз с близкими значениями IC50 1.08 мМ для АХЭ и 0.92 мМ для БХЭ. Описаны детали взаимодействия между форcитозидом Е и холинэстеразами.

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.

форcитозид Еацетилхолинэстеразабутирилхолинэстеразаспектроскопияforsythoside EacetylcholinesterasebutyrylcholinesterasespectroscopyThe study was supported by Natural Science Foundation of Shanxi Province (No. 201801D121290) and the Open Fund from the Key Laboratory of Cellular Physiology (Shanxi Medical University; No. KLMEC/SXMU-201911). We thank Rongrong Gao (College of Chemistry, Nankai University), Yu Li (South China Academy of Advanced Optoelectronics, South China Normal University) and Qin Guo (College of Chemistry and Chemical Engineering, Southwest University) for their advice, technical support and preliminary experiments.ReferencesT. H. Ferreira-Vieira, I. M. Guimaraes, F. R. Silva, F. M. Ribeiro, Curr. Neuropharmacol., 14, 101 (2016).T. H. Ferreira-Vieira, I. M. Guimaraes, F. R. Silva, F. M. Ribeiro, Curr. Neuropharmacol., 14, 101 (2016).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).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).S. S. Xing, Q. Li, B. C. Xiong, Y. Chen, F. Feng, W. Y. Liu, H. P. Sun, Med. Res. Rev., 41, 858 (2020).S. S. Xing, Q. Li, B. C. Xiong, Y. Chen, F. Feng, W. Y. Liu, H. P. Sun, Med. Res. Rev., 41, 858 (2020).H. Dvir, I. Silman, M. Harel, T.L. Rosenberry, J. L. Sussman, Chem. Biol. Interact., 187, 10 (2010).H. Dvir, I. Silman, M. Harel, T.L. Rosenberry, J. L. Sussman, Chem. Biol. Interact., 187, 10 (2010).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).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).M. Mehta, A. Adem, M. Sabbagh, Int. J. Alzheimers Dis., 2012, 728983 (2012).M. Mehta, A. Adem, M. Sabbagh, Int. J. Alzheimers Dis., 2012, 728983 (2012).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).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).P. Anand, B. Singh, Arch. Pharm. Res., 36, 375 (2013).P. Anand, B. Singh, Arch. Pharm. Res., 36, 375 (2013).[CPH] Chinese Pharmacopoeia Commission, Pharmacopoeia of the People’s Republic of China. Part Five, China Medical Science Press, 170 (2020).[CPH] Chinese Pharmacopoeia Commission, Pharmacopoeia of the People’s Republic of China. Part Five, China Medical Science Press, 170 (2020).F. N. Wang, Z. Q. Ma, Y. Liu, Y. Z. Guo, Z. W. Gu, Molecules, 14, 1324 (2009).F. N. Wang, Z. Q. Ma, Y. Liu, Y. Z. Guo, Z. W. Gu, Molecules, 14, 1324 (2009).Y. Li, Q. Guo, Y. Yan, T. Chen, C. Du, H. Du, Spectrochim. Acta A: Mol. Biomol. Spectrosc., 214, 309 (2019).Y. Li, Q. Guo, Y. Yan, T. Chen, C. Du, H. Du, Spectrochim. Acta A: Mol. Biomol. Spectrosc., 214, 309 (2019).X. Yan, T. Chen, L. Zhang, H. Du, Eur. J. Pharmacol., 810, 141 (2017).X. Yan, T. Chen, L. Zhang, H. Du, Eur. J. Pharmacol., 810, 141 (2017).X. Yan, T. Chen, L. Zhang, H. Du, Int. J. Biol. Macromol., 119, 1344 (2018).X. Yan, T. Chen, L. Zhang, H. Du, Int. J. Biol. Macromol., 119, 1344 (2018).M. Georgiev, K. Alipieva, I. Orhan, R. Abrashev, P. Denev, M. Angelova, Food Chem., 128, 100 (2011).M. Georgiev, K. Alipieva, I. Orhan, R. Abrashev, P. Denev, M. Angelova, Food Chem., 128, 100 (2011).B. Ahmad, S. Parveen, R. H. Khan, Biomacromolecules, 7, 1350 (2006).B. Ahmad, S. Parveen, R. H. Khan, Biomacromolecules, 7, 1350 (2006).G. L. Ellman, K. D. Courtney, V. Andres, R. M. Featherstone, Biochem. Pharmacol., 7, 88 (1961).G. L. Ellman, K. D. Courtney, V. Andres, R. M. Featherstone, Biochem. Pharmacol., 7, 88 (1961).R. Li, D. Dhankhar, J. Chen, T. C. Cesario, P. M. Rentzepis, Proc. Natl. Acad. Sci. USA, 116, 18822 (2019).R. Li, D. Dhankhar, J. Chen, T. C. Cesario, P. M. Rentzepis, Proc. Natl. Acad. Sci. USA, 116, 18822 (2019).J. N. Miller, Proc. Anal. Div. Chem. Soc., 16, 203 (1979).J. N. Miller, Proc. Anal. Div. Chem. Soc., 16, 203 (1979).P. D. Ross, S. Subramanian, Biochemistry, 20, 3096 (1981).P. D. Ross, S. Subramanian, Biochemistry, 20, 3096 (1981).U. Anand, C. Jash, S. Mukherjee, J. Phys. Chem. B, 114, 15839 (2010).U. Anand, C. Jash, S. Mukherjee, J. Phys. Chem. B, 114, 15839 (2010).J. R. Lackowicz, Principles of Fluorescence Spectroscopy, 3rd ed., Plenum Press, New York, 603–606 (2006).J. R. Lackowicz, Principles of Fluorescence Spectroscopy, 3rd ed., Plenum Press, New York, 603–606 (2006).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).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).I. M. Klotz, Ann. N. Y. Acad. Sci., 226, 18 (1973).I. M. Klotz, Ann. N. Y. Acad. Sci., 226, 18 (1973).D. Leckband, Annu. Rev. Biophys. Biomol. Struct., 29, 1 (2000).D. Leckband, Annu. Rev. Biophys. Biomol. Struct., 29, 1 (2000).

The authors declare that there are no conflicts of interest present.