Current Enzyme Inhibition最新文献

{"title":"Investigation Of The Potential Antidiabetic Effect Of Zygophyllum Sp. By Studying The Interaction Of Its Chemical Compounds With Alpha-Amylase And Dpp-4 Enzymes Using A Molecular Docking Approach","authors":"S. Bouchentouf, Bouziane Arbi, M. El‐Shazly","doi":"10.2174/1573408019666230202092954","DOIUrl":"https://doi.org/10.2174/1573408019666230202092954","url":null,"abstract":"\u0000\u0000Diabetes type II is one of the most serious metabolic diseases in the world attracting the attention of many researchers who predict that diabetes will be one of the top major causes of disability or death in the coming few decades. To tackle this disease several classes of synthetic molecules were developed to target certain enzymes that are involved in sugar metabolism. Herbal extracts targeting diabetes have witnessed renascence in the last few decades with the introduction of highly effective herbal remedies that effectively regulate sugar levels in the blood.\u0000\u0000\u0000\u0000In this work, we studied the interaction of molecules from the Zygophyllum sp. with the main enzymes involved in sugar metabolism (alpha-amylase and DPP-4) using Molecular Operating Environment (MOE) as a molecular docking technique. The choice of Zygophyllum sp. was based on an ethnopharmacological local survey.\u0000\u0000\u0000\u0000The obtained results showed that myristic acid gave the best score equal to -7.5471 Kcal/mol for alpha-amylase and -9.0457 Kcal/mol for DPP-4. Palmitic acid also gave a good score equal to -7.4528 Kcal/mol with DPP-4.\u0000\u0000\u0000\u0000Conclusion: The calculated scores of molecules from Zygophyllum sp. were better than those calculated with the known inhibitors. The results demonstrated that many molecules showed good affinity to two important enzymes involved in type II diabetes, suggesting that these molecules may possess potential hypoglycemic and antidiabetic effects. These results added further scientific evidence supporting the folk use of Zygophyllum sp. in targeting diabetes and suggested its potential as a valuable source of antidiabetic drug leads.\u0000\u0000\u0000\u0000The obtained results showed that myristic acid gave the best score equal to -7.5471 Kcal/mol for alpha-amylase and -9.0457 Kcal/mol for DPP-4. Palmitic acid gave also a good score equal to -7.4528 Kcal/mol with DPP-4.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2023-02-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41898541","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cholinesterase Aging Phenomenon Following Acute Ethoprophos Poisoning: A Case Report","authors":"B. Chefirat, El Haouaria Touer, Nour El Houda Bensaid, H. Rezk-kallah","doi":"10.2174/1573408019666221221091244","DOIUrl":"https://doi.org/10.2174/1573408019666221221091244","url":null,"abstract":"\u0000\u0000Acute poisoning by Ethoprphos, an organophosphorus pesticide, leads to a veritable cholinergic syndrome whose diagnosis is based on the determination of cholinesterase activity. The treatment relies on the administration of atropine and pralidoxime to regenerate cholinesterases before their ageing.\u0000\u0000\u0000\u0000We report a case of a two-year-old child, hospitalized for ethoprophos poisoning, with seizures associated with tight myosis, bronchial congestion, fever, and sialorrhea. The determination of butyrylcholinesterase and acetylcholinesterase showed low rates throughout the hospitalization. Knowing that pralidoxime was introduced from the 5th day of the poisoning, these rates could be explained by aging of cholinesterases. This phenomenon is well established for organophosphate pesticides (OPs) with methylated or ethyl alkyl groups in contrast to others that are much less documented such as dipropyled OPs such as ethoprophos. The recovery of the enzyme rates was very slow with good clinical improvement.\u0000\u0000\u0000\u0000Ethoprophos poisoning may cause a life-threatening prognosis with a possible phenomenon of cholinesterase aging in the absence of rapid management with administration of pralidoxime.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-12-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43329736","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Syringin as TGF-βR1, HER2, EGFR, FGFR4 kinase, and MMP-2 inhibitor and Potential Cytotoxic Agent Against ER+ Breast Cancer Cells","authors":"R. D. Vasquez, Charlaine A. Aventurado, Agnes L. Castillo","doi":"10.2174/1573408019666221107145705","DOIUrl":"https://doi.org/10.2174/1573408019666221107145705","url":null,"abstract":"\u0000\u0000Breast cancer is currently the most diagnosed cancer worldwide. Neoplastic cells and components of the tumor microenvironment trigger enzymes and receptors to facilitate cancer advancement. Syringin, a natural phenylpropanoid glycoside, has been reported to possess anti-cancer activity and affinity with numerous druggable targets of breast carcinoma\u0000\u0000\u0000\u0000This work aims to evaluate the effects of syringin on the growth of breast cancer cells (MCF-7) and normal dermal fibroblast cells (HDFn) and its ability to inhibit the protein targets of breast cancer.\u0000\u0000\u0000\u0000Syringin was investigated on cell lines in vitro via MTT assay. Using non-cell-based activity assay kits, its influence on the activity of transforming growth factor-beta receptor type 1 (TGF-βR1), human epidermal growth factor receptor (HER2), epidermal growth factor receptor (EGFR), fibroblast growth factor receptor 4 (FGFR4), and matrix metalloproteinase-2 (MMP-2) was evaluated.\u0000\u0000\u0000\u0000Syringin exhibited significant cytotoxicity against MCF-7 cells (IC50: 32.11 µM for 24 hours and 21.35 µM for 48 hours) and was non-toxic on healthy HDFn cells (IC50: >100 µM for 24 and 48 hours). It significantly suppressed the activity of cancer and angiogenesis regulating enzymes in vitro with commendable IC50 values on TGF-βR1 kinase (IC50: 6.48 µM), HER2 kinase (IC50: 7.18 µM), EGFR kinase (IC50: 12.38 µM), FGFR4 kinase (IC50: 16.03 µM), and MMP-2 (IC50: 16.07 µM).\u0000\u0000\u0000\u0000Findings showed the selective toxicity of syringin on breast cancer cells and its potential against pro-angiogenic enzymes. These discoveries strongly indicate the significance and therapeutic potential of syringin in targeted cancer therapy.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-11-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42876313","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Aromatase Enzyme Activity and Liver Receptor Homolog-1 Levels in Gestational Diabetes Mellitus","authors":"N. Bayraktar, Hasip Tas, M. Bayraktar, I. Koyuncu, I. Sari, H. Uyanıkoğlu","doi":"10.2174/1573408019666221103145729","DOIUrl":"https://doi.org/10.2174/1573408019666221103145729","url":null,"abstract":"\u0000\u0000Gestational diabetes mellitus (GDM) is one of the prediabetes conditions in which high blood sugar levels and body weight increase during pregnancy. The underlying molecular and biochemical mechanisms of GDM are poorly defined.\u0000\u0000\u0000\u0000Aromatase enzyme activity is responsible for the conversion of androgens to estrogens and has a share in the regulation of body fat distribution and liver receptor homolog-1 (LRH-1), which plays a critical role in cholesterol transport, acid homeostasis, and steroidogenesis in GDM patients. This study aims to determine the levels of aromatase enzyme and LRH-1 in GDM patients and to investigate the relationship between the levels of aromatase enzyme and LRH-1 and the levels of insulin, HbA 1c and total cholesterol.\u0000\u0000\u0000\u0000This prospective cross-sectional study was conducted over eleven months (September 2020 to July 2021). The study population was selected at Harran University Teaching and Research Hospital. The study included 32 GDM patients and 32 healthy pregnants. The automated assay measured serum fasting blood glucose, HbA1c, and insulin levels (AVIDA 1800 Chemistry System; Siemens). Aromatase enzyme activity and LRH-1 levels were determined by using a commercial enzyme-linked immunosorbent assay (ELISA) kit.\u0000\u0000\u0000\u0000Aromatase activity decreased in GDM patients while LRH1 increased. Significant differences in means levels of fasting blood glucose (p=0.11), insulin (p= 0.001) and HbA1c (p= 0.001) between the patients and control groups. There was a significant negative correlation between the levels of aromatase and insulin (r=-370, p =0.037). In addition, a positive significant correlation coefficient (r=0.645, p=0.001) was found between HbA1c and total cholesterol among the patients' group.\u0000\u0000\u0000\u0000Our findings indicate that there is a negative relationship between aromatase activity and insulin levels. Aromatase and LRH 1 may play a role in the pathogenesis of GDM, and the use of LRH-1 agonists in treating the disease may be considered an alternative treatment in the future. However, additional studies are required to reveal the possible functions of these two proteins in GDM with their mechanisms.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-11-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43348272","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Rational drug design and in vitro cell line studies of some N-(4-(1H-benzo[d]imidazol-2-yl)phenyl)arylamine derivatives as aromatase inhibitors for the treatment of cancer","authors":"P. Sabale, Nusrat B Sayyad","doi":"10.2174/1573408019666221028142316","DOIUrl":"https://doi.org/10.2174/1573408019666221028142316","url":null,"abstract":"\u0000\u0000Aromatase is a catalytic enzyme involved in the biosynthesis of estrogen from androgen. It catalyzes the last rate-limiting/crucial critical step in estrogen biosynthesis. Following the success of the aromatase inhibitor, researchers are working on developing a small physiologically active molecule with fewer side effects and improved tolerance.\u0000\u0000\u0000\u0000Inhibition of the aromatase enzyme, which plays a major role in the rate-limiting phase, is one strategy to prevent estrogen synthesis. After knowing the importance of nitrogen atom containing moieties in the treatment of breast cancer, we have designed some N-(4-(1H-benzo[d]imidazol-2-yl)phenyl)arylamine derivatives through in silico screening such as ADMET analysis and molecular docking studies. From the present investigation we aimed for the synthesis and biological evaluation of the most potent derivatives obtained in this study.\u0000\u0000\u0000\u0000The selected derivatives were synthesized and confirmed by spectral analysis (FTIR, 1H NMR, and Mass). Cytotoxic activity of the compounds was evaluated by colorimetric MTT assay on MDA-MB-231 (breast adenocarcinoma), MCF-7(breast adenocarcinoma), A549 (lung adenocarcinoma) NCI-H23 (Lung carcinoma) and A-498 (Renal carcinoma) cell line using Doxorubicin hydrochloride as positive control.\u0000\u0000\u0000\u0000From present investigation, we have concluded that compound 10 [N-(4-(1H-benzo[d]imidazol-2-yl)phenyl)-1H-benzo[d]imidazol-5-amine) is most potent and exhibited -9.5 kcal/mol binding affinity. It has formed conventional hydrogen bonds with ALA306 and THR310. It displayed most promising activity with GI50 value 0.796±0.06 µM, 0.695±0.05 µM, 1.14±0.06 µM, 2.15±0.04 µM, and 0.987±0.07 µM against MDAMB-231, MCF-7, A-549, NCI-H23, and A-498, respectively when compared with Doxorubicin (0.306±0.04 µM, 0.270±0.02 µM, 0.297±0.04 µM, 0.305±0.04 µM, and 0.345±0.09 µM).\u0000\u0000\u0000\u0000From present investigation it is concluded that the designed molecules had potential to be developed as broad spectrum anticancer agents.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-10-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45699339","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Preface","authors":"Claudiu T. Supuran","doi":"10.2174/157340801901230302122755","DOIUrl":"https://doi.org/10.2174/157340801901230302122755","url":null,"abstract":"<jats:sec>\u0000<jats:title />\u0000<jats:p />\u0000</jats:sec>","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-10-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43056362","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Plant alpha-amylase inhibitors: steady kinetic study, Bidens odorata aqueous infusion toxicity and stability in digestive tract simulation","authors":"R. Valdés, E. P. S. Ceniceros, A. Iliná, J. L. Hernández, Sonia Yesenia Silva Belmares, Rodolfo Ramos González, Raihana Kunakova, R. Zaynullin","doi":"10.2174/1573408018666220929154758","DOIUrl":"https://doi.org/10.2174/1573408018666220929154758","url":null,"abstract":"\u0000\u0000α-Amylase inhibitors are considered an important therapeutic target to control type 2 diabetes mellitus, reducing postprandial hyperglycemia. Medicinal plants are an important source with inhibitory activities of this enzyme, but little studied.\u0000\u0000\u0000\u0000The present study explored the α-amylase inhibition with extracts of 11 medicinal plants available in Saltillo, Mexico; the kinetic mechanism of inhibition of selected extracts and their phytochemical screening; evaluation of the toxicity of Bidens odorata extract in Artemia salina model, as well as estimation of its inhibitory effect under in vitro digestive tract conditions.\u0000\u0000\u0000\u0000The inhibitory assays were carried out spectrophotometrically with aqueous suspensions of the extracts obtained after evaporation of solvent from aqueous and ethanolic infusions.\u0000\u0000\u0000\u0000Eleven plants showed an inhibitory effect of α-amylase above 10% of the initial activity at 666.7 ppm. Four plants were selected for kinetic assay due to inhibitory effect near or higher than 20 %. The IC50 for the aqueous suspension of the ethanolic extract of Bidens odorata was 851 ppm similar to that detected with the drug acarbose. The inhibition mechanism for Bidens odorata, Cinchona succirub, and Opuntia ficus-indicata was competitive, and for Cnidoscolus chayamansa it was uncompetitive. All selected extracts presented flavonoids, the majority contained terpenoids, 3 contained tannins and phenols. The aqueous infusion of Bidens odorata - model of a functional drink, showed no toxicity and was characterized by resistance for 60 min to simulated stomach and intestinal conditions in vitro.\u0000\u0000\u0000\u0000The findings of this study revealed the species of medicinal plants, which were not previously considered as sources of α-amylase inhibitors, and their kinetic mechanisms of inhibition, which can be used for functional hypoglycemic food preparation.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48818427","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"3D-QSAR, Molecular Docking and Pharmacokinetic Studies: In-Silico Approach to Search Novel Inhibitors of 5-Alpha Reductase for Treatment of Benign Prostatic Hyperplasia","authors":"N. Dhingra, Harnoor Kaur, A. Kumari, P. Rana, T. Kaur","doi":"10.2174/1573408018666220914102231","DOIUrl":"https://doi.org/10.2174/1573408018666220914102231","url":null,"abstract":"\u0000\u0000To identify novel steroidal 5-alpha reductase (5AR) inhibitors using computational approaches.\u0000\u0000\u0000\u0000To exploit the steroidal nuclei for possible modifications by creating a library of 17-oximino-5-androsten-3-carboxamide derivatives and identify potent 5AR inhibitors based on docking and pharmacokinetic parameters.\u0000\u0000\u0000\u0000Benign prostatic hyperplasia (BPH), is a condition of aged men, that is characterized by lower urinary tract symptoms. Excessive production of dihydrostestosterone (DHT) from testosterone has been found to play a major role in its pathophysiology. Studies targeting the 5AR enzyme have so far resulted in the development of two clinical approved 5AR inhibitors.\u0000\u0000\u0000\u0000Atom-based three dimensional-quantitative structure activity relationship (3D-QSAR) models have been developed using a selected series of steroidal derivatives as 5AR inhibitors, to elucidate the structural properties required for 5AR inhibitory activities. Further In‒silico studies (molecular docking and pharmacokinetic properties like adsorption, distribution, metabolism, and excretion) of 17-oximino-5-androsten-3-carboxamide derivatives have also been carried out to identify the binding orientation and protein-ligand interactions responsible for the exhibited activity and drug like properties.\u0000\u0000\u0000\u0000The best 3D-QSAR model was generated using Partial Least Square method with an excellent correlation coefficient (R², training set) of 0.882, standard deviation (SD) of 0.09, and a predicted coefficient (Q², test set) of 0.814. Docking analysis indicated that the designed series of compounds have comparable binding affinity from -8.961 to -8.017 to the protein and suggested that hydrophobic and electrostatic moieties can have a key role in the inhibition mechanism.\u0000\u0000\u0000\u00003D-QSAR, molecular docking and pharmacokinetic studies indicated that 17-oximino-5-androsten-3-carboxamide derivatives could be studied further to provide a new strategy for the treatment of BPH.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-09-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44907739","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Synthesis, In-silico and In-vitro Antimycobacterial Studies on Novel Benzofuran\u0000Derivatives","authors":"B. Thorat, D. E. Shelke, S. Dhabarde, Suraj N. Mali","doi":"10.2174/1573408018666220802113450","DOIUrl":"https://doi.org/10.2174/1573408018666220802113450","url":null,"abstract":"\u0000\u0000Benzofurans, an interesting heterocyclic compound, are available abundantly in nature and show a wider range of pharmacological activities. Moreover, in recent years this moeity has been found to have strong antituberculosis potential. Considering the importance of this moiety in the field of medicinal chemistry, we have synthesized a few benzofuran derivatives.\u0000\u0000\u0000\u0000These derivatives were also characterized by standard spectroscopic methods. Synthesized compounds were observed for their anti-tuberculosis activity using microplate Alamar Blue assay (MABA) assay and found to have a minimum of 100 (μg/mL) of minimum inhibitory concentration (MIC) values. Moreover, our molecular docking analyses depicted strong inhibitory potential against a popular TB target, Decaprenylphosphoryl-β-d-ribose 2′-epimerase (DprE1), a crucial enzyme for cell wall synthesis.\u0000\u0000\u0000\u0000Compound 9e was found to have a strong binding energy score of -148.47 kcal/mol against the selected targets (PDB id: 6HEZ).\u0000\u0000\u0000\u0000All compounds were also found to possess drug-likeness characteristics when checked with Lipinski's filter.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-08-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44771817","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Antidiabetic Potential of Ruthenium(III) hydroxamate Complexes:Spectrophotometric Investigations.","authors":"R. Kaushal, Mandeep Kaur","doi":"10.2174/1573408018666220825152849","DOIUrl":"https://doi.org/10.2174/1573408018666220825152849","url":null,"abstract":"\u0000\u0000The 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).\u0000\u0000\u0000\u0000In 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 0.35g/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.\u0000\u0000\u0000\u0000The 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.\u0000\u0000\u0000\u0000All the complexes (except complex 3) exhibited remarkable antiradical activity.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-08-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42032669","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}