{"title":"Antidiabetic Potential of Ruthenium(III) hydroxamate Complexes:Spectrophotometric Investigations.","authors":"R. Kaushal, Mandeep Kaur","doi":"10.2174/1573408018666220825152849","DOIUrl":null,"url":null,"abstract":"\n\nThe potential antidiabetic and antioxidant properties of four ruthenium(III) hydroxamate complexes [RuCl(H2O)(LI-III)2] (1-3) and [RuCl3(H2O)(HLIV)2] (4) were investigated on α-cell enzymes (α-amylase and α-glucosidase).\n\n\n\nIn the instance of -amylase inhibition investigations, the antidiabetic studies of the complexes revealed that they are more active than even the Acarbose as standard, with complex 4 having an IC50 value of 52.31 g/ml. For α-glucosidase inhibition, complex 4 was observed to be the best inhibitor with a remarkable 0.35g/ml IC50 value, which may be attributed to the size and superior lipophilicity of this complex, enabling it to interact with the biological system more effectively than complexes 1-3.The complexes with the best IC50 values were studied further for enzyme kinetics. Molecular docking studies were performed as well to investigate the interactions between the synthesized complexes and target enzymes viz., α glucosidase and α-amylase.\n\n\n\nThe obtained in-vitro results have also been supported by the results of the in-silico docking studies. Furthermore, the antiradical activity of Ru(III) complexes was assessed for its effectiveness in reducing oxidative stress.\n\n\n\nAll the complexes (except complex 3) exhibited remarkable antiradical activity.\n","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":" ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2022-08-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current Enzyme Inhibition","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2174/1573408018666220825152849","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"Pharmacology, Toxicology and Pharmaceutics","Score":null,"Total":0}
引用次数: 0
Abstract
The potential antidiabetic and antioxidant properties of four ruthenium(III) hydroxamate complexes [RuCl(H2O)(LI-III)2] (1-3) and [RuCl3(H2O)(HLIV)2] (4) were investigated on α-cell enzymes (α-amylase and α-glucosidase).
In the instance of -amylase inhibition investigations, the antidiabetic studies of the complexes revealed that they are more active than even the Acarbose as standard, with complex 4 having an IC50 value of 52.31 g/ml. For α-glucosidase inhibition, complex 4 was observed to be the best inhibitor with a remarkable 0.35g/ml IC50 value, which may be attributed to the size and superior lipophilicity of this complex, enabling it to interact with the biological system more effectively than complexes 1-3.The complexes with the best IC50 values were studied further for enzyme kinetics. Molecular docking studies were performed as well to investigate the interactions between the synthesized complexes and target enzymes viz., α glucosidase and α-amylase.
The obtained in-vitro results have also been supported by the results of the in-silico docking studies. Furthermore, the antiradical activity of Ru(III) complexes was assessed for its effectiveness in reducing oxidative stress.
All the complexes (except complex 3) exhibited remarkable antiradical activity.
期刊介绍:
Current Enzyme Inhibition aims to publish all the latest and outstanding developments in enzyme inhibition studies with regards to the mechanisms of inhibitory processes of enzymes, recognition of active sites, and the discovery of agonists and antagonists, leading to the design and development of new drugs of significant therapeutic value. Each issue contains a series of timely, in-depth reviews written by leaders in the field, covering a range of enzymes that can be exploited for drug development. Current Enzyme Inhibition is an essential journal for every pharmaceutical and medicinal chemist who wishes to have up-to-date knowledge about each and every development in the study of enzyme inhibition.