Open Accessα-AMYLASE INHIBITION AND ELECTROCHEMICAL BEHAVIOR OF SOME OXOVANADIUM (IV) COMPLEXES OF L-AMINO ACIDS
Author(s) -
Mahendra Kumar Mishra,
Richik Tripathi,
Pandeya Kb,
Tripathi Ip
Publication year - 2018
Publication title -
asian journal of pharmaceutical and clinical research
Language(s) - English
Resource type - Journals
eISSN - 2455-3891
pISSN - 0974-2441
DOI - 10.22159/ajpcr.2018.v11i8.25800
Subject(s) - amino acid , chemistry , electrochemistry , histidine , redox , solubility , ic50 , metal , medicinal chemistry , inorganic chemistry , in vitro , organic chemistry , biochemistry , electrode
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.