α-AMYLASE INHIBITION AND ELECTROCHEMICAL BEHAVIOR OF SOME OXOVANADIUM (IV) COMPLEXES OF L-AMINO ACIDS

  • Mahendra Kumar Mishra Department of Biological Sciences, Mahatma Gandhi Chitrakoot Gramodaya Vishwavidyalaya, Chitrakoot, Satna, Madhya Pradesh, India. http://orcid.org/0000-0002-9380-8943
  • Ruchita Tripathi Department of Biotechnology, Govt. T. R. S. College, Rewa Madhya Pradesh, India.
  • Pandeya Kb Department of Physical Sciences, Mahatma Gandhi Chitrakoot Gramodaya Vishwavidyalaya, Chitrakoot, Satna, Madhya Pradesh, India.
  • Tripathi Ip Department of Faculty of Science and Environment, Mahatma Gandhi Chitrakoot Gramodaya Vishwavidyalaya, Chitrakoot, Satna, Madhya Pradesh, India.

Abstract

Objective: Diabetes is complex metabolic disease having a symptom of hyperglycemia. Oxovanadium (IV) and l-amino acids are used to normalize the hyperglycemic condition. The aim of this study was to screen the α-amylase inhibitory activity of l-amino acids, their oxovanadium (IV) complexes, and electrochemical activity of oxovanadium (IV) complexes.

Methods: All the oxovanadium (IV) complexes were synthesized according to the solubility of l-amino acids; the molar ratio of metal to l-amino acid was 1:2. The synthesized oxovanadium (IV) complexes were examined for their electrochemical behavior in 0.01 M sodium perchlorate solution. Further, the oxovanadium (IV) complexes of l-amino acids and l-amino acids were screened for their α-amylase inhibitory activity using spectrophotometric assay system.

Results: The synthesized complexes were divided into four groups according to nature of amino acids. Entire complexes show simple irreversible wave for VO redox couples in −900–50 mV potential range and scan rate was 300 mV/S. All the complexes and l-amino acids were screened for their α-amylase inhibitory activity. L-Histidine and their oxovanadium (IV) complex show the minimum IC50 value, i.e. 4199.05 μM and 101.015 μM, respectively, in their respective groups.

Conclusion: The data obtained from our study, it reveals that the entire oxovanadium (IV) complexes are an irreversible wave for VO redox system and the l-histidine and its oxovanadium (IV) complex is the most potent inhibitor for the α-amylase. Further, the complexes show minimum IC50 value on comparing their respective ligands due to the interaction of Vanadyl complex to the enzyme, at the sixth vacant position of Vanadyl complex.

Keywords: Diabetes mellitus, Oxovanadium (IV) complexes, l-Amino acids, α-amylase inhibition, Cyclic voltammeter.

Author Biography

Mahendra Kumar Mishra, Department of Biological Sciences, Mahatma Gandhi Chitrakoot Gramodaya Vishwavidyalaya, Chitrakoot, Satna, Madhya Pradesh, India.

Research Associate

Dept of Chemistry

References

1. Henriksen EJ, Diamond-Stanic MK, Marchionne EM. Oxidative stress and the etiology of insulin resistance and Type 2 diabetes. Free Radic Biol Med 2010;51:993-9.
2. Gruenwald J, Freder J, Armbruester N. Cinnamon and health. Crit Rev Food Sci Nutr 2010;50:822-34.
3. Adeghate E, Schattner P, Dunn E. An update on the etiology and epidemiology of diabetes mellitus. Ann N Y Acad Sci 2006;1084:1-29.
4. Kalsi A, Singh S, Taneja N, Kukal S, Mani S. Current treatments for Type 2 diabetes, their side effects and possible complementary treatments. Int J Pharm Pharm Sci 2015;7:14-8.
5. Smyth S, Heron A. Diabetes and obesity: The twin epidemics. Nat Med 2006;12:75-80.
6. Lee Y, Berglund ED, Yu X, Wang MY, Evans MR, Scherer PE, et al. Hyperglycemia in rodent models of Type 2 diabetes requires insulin resistant alpha cells. Proc Natl Acad Sci U S A 2014;111:13217-22.
7. Ramasubbu N, Paloth V, Luo Y, Brayer GD, Levine MJ. Structure of human salivary alpha-amylase at 1.6 a resolution: Implications for its role in the oral cavity. Acta Crystallogr Sect D Biol Crystallogr 1996;52:435-46.
8. Butterworth PJ, Warren FJ, Ellis PR. Human alpha-amylase and starch digestion: An interesting marriage. Starch J 2011;63:395-405.
9. Inzucchi SE, Bergenstal RM, Buse JB, Diamant M, Ferrannini E, Nauck M, et al. Management of hyperglycaemia in Type 2 diabetes, 2015: A patient-centred approach. Update to a position statement of the American diabetes association and the European association for the study of diabetes. Diabetologia 2015;58:429-42.
10. Nichols BL, Avery S, Sen P, Swallow DM, Hahn D, Sterchi E. The maltase-glucoamylase gene: Common ancestry to sucrase-isomaltase with complementary starch digestion activities. Proc Natl Acad Sci USA 2003;100:1432-7.
11. Sels JP, Huijberts MS, Wolffenbuttel BH. Miglitol, a new alpha-glucosidase inhibitor. Expert Opin Pharmacother 1999;1:149-56.
12. Van de Laar FA. Alpha-glucosidase inhibitors in the early treatment of Type 2 diabetes. Vasc. Health Risk Manag 2008;4:1189-95.
13. Baron AD. Postprandial hyperglycaemia and alpha-glucosidase inhibitors. Diabetes Res Clin Pract 1998;40 Suppl:S51-5.
14. Panchal I, Sen DJ, Navle A, Shah U. Structure-based drug designing, scoring, and synthesis of some substituted sulphonylureas/guanidine-based derivatives as hypoglycemic agents. Int J Pharm Pharm Sci 2017;9:226-32.
15. Vichayanrat A, Ploybutr S, Tunlakit M, Watanakejorn P. Efficacy and safety of voglibose in comparison with acarbose in Type 2 diabetic patients. Diabetes Res Clin Pract 2002;55:99-103.
16. Pandeya KB, Tripathi IP, Mishra MM, Jaiswal N. Antiradical and antioxidant properties of some oxovanadium(IV) complexes of l-amino acids. J Biol Sci Med 2016;2:38-47.
17. Boivin M, Flourie B, Rizza RA, Go VL, DiMagno EP. Gastrointestinal and metabolic effects of amylase inhibition in diabetics. Gastroenterology 1988;94:387-94.
18. Apostolidis E, Lee CM. In vitro potential of Ascophyllum nodosum phenolic antioxidant-mediated α-glucosidase and α-amylase inhibition. J Food Sci 2010;75:H97-H102.
19. Zou KH, Tuncali K, Silverman SG. Correlation and simple linear regression. Radiology 2003;227:617-28.
20. Lyonnet B, Martz M, Martin E. L’emploi therapeutique des derives du vanadium. La Presse Med 1899;1:191-2.
21. Willsky GR, Chi LH, Godzala M 3rd, Kostyniak PJ, Smee JJ, Trujillo AM, et al. Anti-diabetic effects of a series of vanadium dipicolinate complexes in rats with streptozotocin-induced diabetes. Coord Chem Rev 2011;255:2258-69.
22. Missaoui S, Rhouma KB, Yacoubi MT, Sakly M, Tebourbi O. Vanadyl sulfate Treatment stimulates proliferation and regeneration of beta cells in pancreatic islets. J Diabetes Res 2014;2014. DOI: 10.1155/2014/540242.
23. Thomas S, Jose AG, Quoc-Tuan D, Philippe B, Stefan L. Why antidiabetic vanadium complexes are not in the pipeline of “big pharma” drug research? a critical review. Curr Med Chem 2016;23:2874-91.
24. Adam AM, Naglah AM, Al-Omar MA, Refat MS. Synthesis of a new insulin-mimetic antidiabetic drug containing vitamin A and vanadium(IV) salt: Chemico-biological characterizations. Int J Immunopathol Pharmacol 2017;30:272-81.
25. Thompson MR. The role of amino acids in health and disease. Westchester Med Bull 1946;14:9-14.
26. Tessari P, Cecchet D, Cosma A, Puricelli L, Millioni R, Vedovato M, et al. Insulin resistance of amino acid and protein metabolism in Type 2 diabetes. Clin Nutr 2011;30:267-72.
27. Al-Abbasi FA. Trend analysis of the correlation of amino acid plasma profile with glycemic status in Saudi diabetic patients. J Adv Res 2012;3:305-13.
28. van Loon LJ, Margriet K, Paul PC, Anton JM, Wim HM, Hans AK. Amino acid ingestion strongly enhances insulin secretion in patients with long-term Type 2 diabetes. Diabetes Care 2003;26:625-30.
29. Natarajan SK, Lakshmi S, Punitham R, Arokiasamy T, Sukumar B, Ramakrishnan S. Effect of oral supplementation of free amino acids in Type 2 diabetic patients--a pilot clinical trial. Med Sci Monit 2002;8:CR131-7.
30. Krause MS, McClenaghan NH, Flatt PR, de Bittencourt PI, Murphy C, Newsholme P, et al. L-arginine is essential for pancreatic β-cell functional integrity, metabolism and defense from inflammatory challenge. J Endocrinol 2011;211:87-97.
31. de melo Borges E, Da Silvera Gomes A, Carvalho I. α-and β-glucosidase inhibitors: Chemical structure and biological activity. Tetrahedron 2006;62:10277-302.
32. Niwa T, Doi U, Osawa T. Inhibitory activity of corn-derived bis-amide compounds against alpha-glucosidase. J Agric Food Chem 2003;51:90 4.
33. Madeswaran A, Umamaheswari M, Asokkumar K, Sivashanmugam T, Subhadradevi V, Jagannath P. Computational drug discovery of potential TAU protein kinase I inhibitors using in silico docking studies. Bangladesh J Pharmacol 2013;8:131-5.
34. Misra S, Pandeya KB, Tiwari A, Ali AZ, Saradamani T. α-glucosidase inhibition and DPPH free radical scavenging by oxovanadium(IV) complexes of some tetradentate schiff bases. J Indian Chem Soc 2011;88:1195-201.
35. Cornman CR, Zovinka EP, Meixner MH. Vanadium(IV) complexes of an active-site peptide of a protein tyrosine phosphate. Inorg Chem 1995;34:5099-100.
36. Ptlugrath JW, Wiegand G, Huber R, Vértesy L. Crystal structure determination, refinement and the molecular model of the α-amylase inhibitor Hoe-467A. J Mol Biol 1986;189:383-6.
37. Kline AD, Braun W, Wuthrich K. Determination of the complete three-dimensional structure of the α-amylase inhibitor tendamistat in aqueous solution by nuclear magnetic resonance and distance Geometry. J Mol Biol 1988;204:675-724.
38. Wiegand G, Epp O, Huber R. The crystal structure of porcine pancreatic α-amylase in complex with the microbial inhibitor tendamistat. J Mol Biol 1995;247:99-110.
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Mishra, M. K., R. Tripathi, P. Kb, and T. Ip. “α-AMYLASE INHIBITION AND ELECTROCHEMICAL BEHAVIOR OF SOME OXOVANADIUM (IV) COMPLEXES OF L-AMINO ACIDS”. Asian Journal of Pharmaceutical and Clinical Research, Vol. 11, no. 8, Aug. 2018, pp. 218-24, doi:10.22159/ajpcr.2018.v11i8.25800.
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