Electrochemical assessment of α-amylase inhibition by type 2 diabetes drugs: a cyclic voltammetry study

Short communication

Authors

  • Touhami Lanez University of El Oued, Faculty of Sciences, Chemistry Department, VTRS Laboratory, El Oued, Algeria https://orcid.org/0000-0002-3978-7635
  • Elhafnaoui Lanez University of El Oued, Faculty of Nature and Life Sciences, Cellular and Molecular Biology, Department, VTRS Laboratory, El Oued, Algeria https://orcid.org/0000-0002-6543-2547
  • Aicha Adaika University of El Oued, Faculty of Nature and Life Sciences, Cellular and Molecular Biology, Department, VTRS Laboratory, El Oued, Algeria https://orcid.org/0000-0002-7829-709X

DOI:

https://doi.org/10.5599/jese.2867

Keywords:

Enzyme-starch mixture, IC50, electrochemical assay, antidiabetic agents

Abstract

A new sensitive cyclic voltammetry method was developed for measuring the α-amylase inhibitory activity of six antidiabetic drugs commonly prescribed for type 2 diabetes: acarbose, amaryl, repaglinide, diamecron, dapagliflozin, and metformin. The electro­chemical response of an enzyme-starch mixture was measured in the absence and presence of these drugs. Results indicated varying inhibitory potencies with IC50 values ranging from 6.770 to 41.423 µM, with acarbose as the most potent. UV-Vis absorption spectroscopy at 580 nm validated the cyclic voltammetry results, with very good concordance. This study highlights the utility of electrochemical assays for the rapid, quantitative screening of α-amylase inhibitors and supports their integration with spectroscopic methods for the evaluation of antidiabetic drugs.

Downloads

Download data is not yet available.

References

[1] U. Galicia-Garcia, A. Benito-Vicente, S. Jebari, A. Larrea-Sebal, H. Siddiqi, K.B. Uribe, H. Ostolaza, C. Martín, Pathophysiology of Type 2 Diabetes Mellitus, International Journal of Molecular Sciences 21 (2020) 6275. https://doi.org/10.3390/ijms21176275

[2] N. A. ElSayed, G. Aleppo, R. R. Bannuru, D. Bruemmer, B. S. Collins, L. Ekhlaspour, J. L. Gaglia, M. E. Hilliard, E. L. Johnson, K. Khunti, I. Lingvay, G. Matfin, R. G. McCoy, M. Lou Perry, S. J. Pilla, S. Polsky, P. Prahalad, R. E. Pratley, A. R. Segal, J. J. Seley, E. Selvin, R. C. Stanton, R. A. Gabbay, 2. Diagnosis and Classification of Diabetes: Standards of Care in Diabetes-2024, Diabetes Care 47(Suppl 1) (2024) S20-S42. https://dx.doi.org/10.2337/dc24-S002

[3] A. Ceriello, Postprandial hyperglycemia and diabetes complications: Is it time to treat? Diabetes 54 (2005) 1-7. https://doi.org/10.2337/diabetes.54.1.1

[4] K. Node, T. Inoue, Postprandial hyperglycemia as an etiological factor in vascular failure, Cardiovascular Diabetology 8 (2009) 23. https://doi.org/10.1186/1475-2840-8-23

[5] D. L. Eizirik, F. Szymczak, R. Mallone. why does the immune system destroy pancreatic β-cells but not α-cells in type 1 diabetes? Nature Reviews Endocrinology 19 (2023) 425-434. https://doi.org/10.1038/s41574-023-00826-3

[6] P. Sudha, S.S. Zinjarde, S.Y. Bhargava, A.R. Kumar, Potent α-amylase inhibitory activity of Indian Ayurvedic medicinal plants, BMC Complementary Medicine and Therapies 11 (2011) 5. https://doi.org/10.1186/1472-6882-11-5

[7] H. E. Lebovitz, Alpha-glucosidase inhibitors, Endocrinology and Metabolism Clinics of North America 26 (1997) 539-551. https://doi.org/10.1016/S0889-8529(05)70266-8

[8] R. Tundis, M. R. Loizzo, F. Menichini, Natural Products as α-amylase and α-glucosidase Inhibi¬tors and their Hypoglycaemic Potential in the Treatment of Diabetes: An Update, Mini-Reviews in Medicinal Chemistry 10 (2010) 315-331. http://dx.doi.org/10.2174/138955710791331007

[9] F. Laar. Alpha-glucosidase inhibitors in the early treatment of type 2 diabetes, Vascular Health and Risk Management 4 (2008) 1189-1195. https://doi.org/10.2147/VHRM.S3119

[10] K. Ninomiya, S. Ina, A. Hamada, Y. Yamaguchi, M. Akao, F. Shinmachi, H. Kumagai, H. Kumagai, Suppressive effect of the α-amylase inhibitor albumin from buckwheat (Fagopyrum esculentum Moench) on postprandial hyperglycaemia, Nutrients 10 (2018) 1503. https://doi.org/10.3390/nu10101503

[11] L. Guo, J. Xia, S. Yu, J. Yan, F. He, M. Zhang, Q. Fan, R. Yang, W. Zhao, Natural edible materials made of protein-functionalized aerogel particles for postprandial hyperglycemia management, International Journal of Biological Macromolecules 167 (2021) 279-288. https://doi.org/10.1016/j.ijbiomac.2020.11.186

[12] J. L. Chiasson, R. G. Josse, R. Gomis, M. Hanefeld, A. Karasik, M. Laakso, Acarbose for prevention of type 2 diabetes mellitus: The STOP-NIDDM randomised trial, The Lancet 359 (2002) 2072-2077. https://doi.org/10.1016/s0140-6736(02)08905-5

[13] G. L. Miller, Use of Dinitrosalicylic Acid Reagent for Determination of Reducing Sugar, Analytical Chemistry 31 (1959) 426-428. https://doi.org/10.1021/ac60147a030

[14] P. Bernfeld, Amylases, α and β, in Methods in Enzymology, S. P. Colowick, N.O. Kaplan, Eds., Academic Press, New York, United States, 1955, pp. 149-158. https://doi.org/10.1016/0076-6879(55)01021-5

[15] D. R. Thévenot, K. Toth, R. A. Durst, G. S. Wilson, Electrochemical biosensors: Recommended definitions and classification, Biosensors and Bioelectronics 16 (2001) 121-131. https://doi.org/10.1016/S0956-5663(01)00115-4

[16] J. Wang, Electrochemical biosensors: Towards point-of-care cancer diagnostics. Biosensors and Bioelectronics 21 (2006) 1887-1892. https://doi.org/10.1016/j.bios.2005.10.027

[17] M. Bae, N. Kim, E. Cho, T. Lee, J.-H. Lee, Recent Advances in Electrochemical Biosensors for Neurodegenerative Disease Biomarkers, Biosensors 15 (2025) 151. https://doi.org/10.3390/bios15030151

[18] S. Li, K. Kerman, Electrochemical biosensors for biometal-protein interactions in neurodegenerative diseases, Biosensors and Bioelectronics 179 (2021) 113035. https://doi.org/10.1016/j.bios.2021.113035

[19] K. Yokoyama, Y. Kayanuma, Cyclic Voltammetric Simulation for Electrochemically Mediated Enzyme Reaction and Determination of Enzyme Kinetic Constants, Analytical Chemistry 70 (1998) 3368-3376. https://doi.org/10.1021/ac9711807

[20] M. Mohiuddin, D. Arbain, A.K.M.Shafiqul Islam, M. S. Ahmad, M. N. Ahmad, Alpha-Glucosidase Enzyme Biosensor for the Electrochemical Measurement of Antidiabetic Potential of Medicinal Plants, Nanoscale Research Letters 11 (2016) 95. https://doi.org/10.1186/s11671-016-1292-1

[21] Z. Xiao, R. Storms, A. Tsang, A quantitative starch-iodine method for measuring alpha-amylase and glucoamylase activities, Analytical Biochemistry 351(1) (2006) 146-148. https://doi.org/10.1016/J.AB.2006.01.036

[22] L. Mogole, W. Omwoyo, F. Mtunzi, Phytochemical screening, anti-oxidant activity and α-amylase inhibition study using different extracts of loquat (Eriobotrya japonica) leaves, Heliyon 6 (2020) e04736. https://doi.org/10.1016/J.HELIYON.2020.E04736

[23] M. Somogyi, Determination of blood sugar, Journal of Biological Chemistry 160 (1945) 69-73. https://doi.org/10.1016/S0021-9258(18)43098-0

[24] Y. Bekkar, E. Lanez, T. Lanez, L. Bourougaa, A. Adaika, A. Benine, Z. Saada, Combined In Vitro and In Silico analysis of ferrocenylmethylaniline derivatives: Antibacterial potential, DFT calculations, and molecular dynamics insights, Journal of Organometallic Chemistry 1032 (2025) 123618. https://doi.org/10.1016/J.JORGANCHEM.2025.123618

[25] X.-W. Yang, M.-Z. Huang, Y.-S. Jin, L.-N. Sun, Y. Song, H.-S. Chen, Phenolics from Bidens bipinnata and their amylase inhibitory properties, Fitoterapia 83 (2012) 1169-1175. https://doi.org/10.1016/j.fitote.2012.07.005

[26] G. Zengin, C. Sarikurkcu, A. Aktumsek, R. Ceylan, O. Ceylan, A comprehensive study on phytochemical characterization of Haplophyllum myrtifolium Boiss. endemic to Turkey and its inhibitory potential against key enzymes involved in Alzheimer, skin diseases and type II diabetes, Industrial Crops and Products 53 (2014) 244-251. https://doi.org/10.1016/j.indcrop.2013.12.043

[27] V. A. Stenger, J. D. McLean, R. M. Van Effen, Polarographic Methods in the Testing of Reagent Chemicals, Analytical Chemistry 57 (1985) 27A-36A. https://doi.org/10.1021/ac00279a716

[28] I. Kosta, H. Grande, R. Tena-Zaera, Dimethylformamide-free processing of halide perovskite solar cells from electrodeposited PbI2 precursor films, Electrochimica Acta 246 (2017) 1193-1199. https://doi.org/10.1016/j.electacta.2017.06.104

[29] I. S. El-Hallag, Electrochemical oxidation of iodide at a glassy carbon electrode in methylene chloride at various temperatures, Journal of the Chilean Chemical Society 55 (2010) 67-73. http://dx.doi.org/10.4067/S0717-97072010000100016

[30] R. Greef, L. M. Peat, L. M. Peter, D. Pletcher, J. Robinson, Instrumental Methods in Electrochemistry, Ellis Horwood, New York, United States, 1990, p. 188. ISBN 978-0745803692.

Downloads

Published

02-11-2025

Issue

Vol. 16 (2026)

Section

Bioelectrochemistry

License

Copyright (c) 2025 Touhami Lanez, Elhafnaoui Lanez, Aicha Adaika

Creative Commons License

This work is licensed under a Creative Commons Attribution 4.0 International License.

How to Cite

Electrochemical assessment of α-amylase inhibition by type 2 diabetes drugs: a cyclic voltammetry study: Short communication. (2025). Journal of Electrochemical Science and Engineering, 16, Article 2867. https://doi.org/10.5599/jese.2867