Effects of Thymol and Carvacrol on Acetylcholinesterase from Drosophila melanogaster

• Authors: H. Askin , M. Yildiz , A. Ayar
• Languages of publication: EN

Abstracts

EN

In this study, inhibitor effects of thymol and carvacrol were investigated in vivo and in vitro on acetylcholinesterase enzyme of Drosophila melanogaster. IC₅₀ values, Ki constants and inhibition types were determined for the substances displaying inhibitory effect. In vivo studies, were performed on larvaes by considering IC₅₀ values. The surviving and mortality rates were determined for the solution applied to larvaes. IC₅₀ values of thymol and carvacrol were found to be 25 mM and 0.175 mM, respectively. By using Lineweaver-Burk graphs, it was found that both compounds show non-competitive type of inhibition. According to results, it was concluded that carvacrol is a more effective inhibitor than thymol. We believe that these findings will contribute to the development of more potent, specific and effective inhibitors against AChE enzyme, design of new drugs for treating Alzheimer's disease and studies in pharmacological applications.

Keywords

EN

42.62.Be

Discipline

• 42.62.Be: Biological and medical applications(see also 87.50.W-, 87.63.L-, and 87.80.Cc in biological and medical physics)

• Publisher: Institute of Physics, Polish Academy of Sciences
• Journal: Acta Physica Polonica A
• Year: 2017
• Volume: 132
• Issue: 3
• Pages: 720-722

Dates

published

2017-09

Contributors

author

H. Askin

• Department of Molecular Biology and Genetics, Faculty of Science, Ataturk University, Erzurum, Turkey

author

M. Yildiz

• Department of Molecular Biology and Genetics, Faculty of Science, Ataturk University, Erzurum, Turkey

author

A. Ayar

• Sabuncuoğlu Şerefeddin Health Services Vocational School, Amasya University, Amasya, Turkey

References

• [1] D.M. Quinn, Chem. Rev. 87, 955 (1987), doi: 10.1021/cr00081a005
• [2] S. Dall'Acqua, Botanics: Targets Therapy 3, 19 (2013), doi: 10.2147/btat.s17297
• [3] K.H. Baser, Current Pharmaceut. Des. 14, 3106 (2008), doi: 10.2174/138161208786404227
• [4] L.T. Reiter, L. Potocki, S. Chien, M. Gribskov, E. Bier, Genome Res. 11, 1114 (2001), doi: 10.1101/gr.169101
• [5] S. Lenz, P. Karsten, J.B. Schulz, A. Voigt, J. Neurochem. 127, 453 (2013), doi: 10.1111/jnc.12446
• [6] Y.M. Hsiao, J.Y. Lai, H.Y. Liao, H.T. Feng, J. Agricult. Food Chem. 52, 5340 (2004), doi: 10.1021/jf0494377
• [7] G.L. Ellman, K.D. Courtney, V. Andes, R.M. Featherstone, Biochem. Pharmacol. 7, 88 (1961), doi: 10.1016/0006-2952(61)90145-9
• [8] H. Lineweaver, D. Burk, J. Am. Chem. Soc. 56, 658 (1934), doi: 10.1021/ja01318a036

Identifiers

DOI

10.12693/APhysPolA.132.720