α-AMYLASE INHIBITION AND ELECTROCHEMICAL BEHAVIOR OF SOME OXOVANADIUM (IV) COMPLEXES OF L-AMINO ACIDS
DOI:
https://doi.org/10.22159/ajpcr.2018.v11i8.25800Keywords:
Diabetes mellitus, Oxovanadium (IV) complexes, l-Amino acids, Nil, Cyclic voltammeterAbstract
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.
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