Current Enzyme Inhibition最新文献

{"title":"Antioxidant and antidiabetic activities of aqueous and methanolic extracts from Athamanta sicula L.","authors":"K. Loucif, Fatima Benchikh, Chawki Ben Souici, Smain Amira","doi":"10.2174/1573408018666220804121440","DOIUrl":"https://doi.org/10.2174/1573408018666220804121440","url":null,"abstract":"\u0000\u0000Oxidative stress plays a major role in the development of diabetes complications; therefore, it is possible to use natural antioxidants as therapeutic agents for diabetes.\u0000\u0000\u0000\u0000This study aimed to find an important source of phenolics from Athamanta sicula L. (A. sicula) and confirm that this plant could be a significant source of medically important natural compounds, by confirming its antioxidant, α-amylase and α-glucosidase inhibitory potential.\u0000\u0000\u0000\u0000Antioxidant property was performed using 2,2′-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging, metal chelating, and cupric reducing antioxidant capacity methods. The α-amylase and α-glucosidase inhibitory activities were investigated using an in vitro model. Moreover, polyphenols and flavonoids contents of the tested extracts were carried out.\u0000\u0000\u0000\u0000The methanolic extract exhibited the highest phenolic and flavonoids content compared to aqueous extract. However, aqueous extract possessed the strongest antioxidant activity (DPPH scavenging, metal chelating, and Cupric ion reducing antioxidant capacities), α-amylase and α-glucosidase inhibitory effects. No correlation between phenolics content and antioxidant and enzyme inhibitory activities of A. sicula L. extracts was observed.\u0000\u0000\u0000\u0000The results showed that this plant could be a significant source of medically important natural compounds.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-08-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44940147","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":"In vitro examination of antioxidant and anti-cholinesterase effects of Athamanta sicula L. aqueous and methanolic extracts","authors":"K. Loucif, Hassiba Benabdallah, Fatima Benchikh, C. Bensouici, Smain Amira","doi":"10.2174/1573408017666220713100342","DOIUrl":"https://doi.org/10.2174/1573408017666220713100342","url":null,"abstract":"\u0000\u0000Oxidative stress plays a critical role in the pathological process of Alzheimer’s disease (AD). There is a growing interest in natural anti-oxidants and cholinesterase inhibitors from medicinal plants that may aid in the prevention against oxidative injury and in the treatment of AD. Athamanta sicula L. is an important medicinal plant.\u0000\u0000\u0000\u0000The aim of current study was to investigate the total phenolic content, antioxidant and anti-cholinesterase properties of aqueous (AqE) and methanolic extracts (MethE) from Athamanta sicula L. (A. sicula L.).\u0000\u0000\u0000\u0000The phenanthroline, ABTS free radical scavenging, β-carotene bleaching methods were utilized to assess the antioxidant capacity. Acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibitory methods were used to determine the anti-cholinesterase effect.\u0000\u0000\u0000\u0000These extracts were rich in phenolic contents. It was capable of scavenging free radicals, inhibiting lipid peroxidation, and reducing agents. A. sicula L. had a remarkable cholinesterase inhibitory effect.\u0000\u0000\u0000\u0000These results support that A. sicula L. could be a new source of anti-oxidant and anti-cholinesterase natural drugs. Further studies on the isolation and characterization of active principles of anti-oxidant and tyrosinase inhibitory activities are needed.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-07-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44897131","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":"Meet the Editorial Board Member","authors":"Z. Alothman","doi":"10.2174/157340801802220825114431","DOIUrl":"https://doi.org/10.2174/157340801802220825114431","url":null,"abstract":"He obtained his Ph.D. in chemistry Oklahoma University in 2006. He is working on a variety of topics ranging from the high surface area materials, Water treatment and production, Ion exchanger, separation and Environmental studies. He is the group leader of Advanced Materials and Chromatography Group and the supervisor of the Advanced Materials Re-search Chair. He supervised seven PhD students and more than 12 master students. He is an author and co-author of more than 350 scientific publications, three books and six patents.","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42402003","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":"Effects of p-Hydroxybenzaldehyde, Vanillin, and Syringaldehyde on Protein Tyrosine Phosphatase 1B Activity","authors":"Joy Atule Peter, A. Olatunde, S. Aminu, I. Umar, A. Mohammed","doi":"10.2174/1573408018666220630140400","DOIUrl":"https://doi.org/10.2174/1573408018666220630140400","url":null,"abstract":"\u0000\u0000The PTP 1B is a negative regulator of insulin signal transduction and hence, serves as a therapeutic target in the treatment of diabetes.\u0000\u0000\u0000\u0000The present study investigated the inhibitory effects of p-hydroxybenzaldehyde, vanillin, and syringaldehyde on the activity of protein tyrosine phosphatases phosphatase 1B (PTP 1B) in vitro.\u0000\u0000\u0000\u0000The PTP 1B inhibitory assay and mode of inhibition of the three compounds were determined using p-nitrophenyl phosphate (p-NPP) in a 96 well microplate. Molecular docking was used to predict the binding affinities of the compounds with the PTP 1B.\u0000\u0000\u0000\u0000The results showed that syringaldehyde exhibited significantly (p< 0.05) higher PTP 1B inhibitory activity (IC50: 12.75 µM) compared to p-hydroxybenzaldehyde (IC50: 33.79 µM) and vanillin (IC50: 42.82 µM) as well as the standards suramin (IC50: 28.35 µM) and ursolic acid (IC50: 19.45 µM). Syringaldehyde and vanillin showed uncompetitive inhibition whereas, p-hydroxybenzaldehyde showed a mixed inhibition type. The molecular docking simulation predicted negative binding energies of -5.0 kcal/mol, -5.5 kcal/mol, and -5.5 kcal/mol for p-hydroxybenzaldehyde, vanillin, and syringaldehyde respectively.\u0000\u0000\u0000\u0000Syringaldehyde showed higher inhibition of PTP 1B compared to other phenolic aldehydes and could be the mechanism of its antidiabetic activity. Hence, further studies are warranted to confirm the efficacy and toxicity of the compound\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46335812","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":"In-silico design,synthesis and evaluation of hydroxyxanthone derivatives as potential anti-diabetic agents targeting α - glucosidase","authors":"Riya Saikia, Aparoop Das, K. Pathak, Neelutpal Gogoi, Tirna Paul, J. Sahariah, H. Sarma","doi":"10.2174/1573408018666220627114552","DOIUrl":"https://doi.org/10.2174/1573408018666220627114552","url":null,"abstract":"\u0000\u0000Glucosidase is a catalytic enzyme that catalyzes, specifically hydrolyses, the carbohydrates to free glucose units in blood in the last step of carbohydrate metabolism. So far, many compounds with α-glucosidase inhibitory activity for example, acarbose, voglibose etc., have been accounted and commercialized for diabetes therapy. However, Xanthones are recognized as efficient glucosidase inhibitors because of their planar structure and thereby opens the door for the researchers to utilize the same for designing and developing potent and novel hybrid xanthones for anti-diabetic therapy.\u0000\u0000\u0000\u0000The current study aimed to determine and evaluate the anti-diabetic potential of different synthetic hydroxylxanthone derivatives using Nicotinamide and Streptozotocin(60mg/kg i.p.) induced diabetic rats.\u0000\u0000\u0000\u0000The partially purified synthetic hydroxyxanthone derivatives namely A1,A2, A3, A4, and A5 were administered to diabetic rats with a dose of 150mg/kg, per oral(p.o.) and the effect of the fraction on blood glucose level was studied upto 21 days. Further, the synthetic compounds were subjected to spectral analysis for their characterization.\u0000\u0000\u0000\u0000The in-silico molecular docking results indicated that the compound A3 has shown the best binding energy score. Also, the in-vivo anti-diabetic potential of the synthetic hydroxyxanthone derivatives have revealed that the compounds A3 and A2 were significantly effective in controlling the blood glucose level when compared to the standard drug miglitol. In addition, compounds A3 and A2 were found to be effective in restoring the enzymes of liver and lipid profile in Streptozotocin-induced Wistar rat models.\u0000\u0000\u0000\u0000With an objective to investigate the compounds for predicting biological activity, it was found that the hydroxyxanthonepossesses a safety margin for toxicity and acts as a lead towards the development of potential α-glucosidase inhibitors. These compounds show excellent correlation between docking results, synthetic data and in-vivo anti-diabetic activity. However, further modifications can be done to enhance the potency, binding affinity profile and minimize toxicity.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-06-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41880956","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":"Antioxidant activity and inhibitory effect of curcumin on some enzymes involved in several diseases: Acetylcholinesterase, butyrylcholinesterase, α-glucosidase and tyrosinase","authors":"Seghira Bisset, W. Sobhi, C. Bensouici, A. Khenchouche","doi":"10.2174/1573408018666220602091615","DOIUrl":"https://doi.org/10.2174/1573408018666220602091615","url":null,"abstract":"\u0000\u0000This study aims the investigation of the potential effect of pure curcumin on the inhibition of different enzymes which are involved in several diseases.\u0000\u0000\u0000\u0000Several chronic diseases such as Alzheimer’s, diabetes, and Parkinson’s disease are related to oxidative stress and enzyme activity. Today, various plant origin products are stated as beneficial against several chronic diseases with secondary metabolites such as phenolic compounds. Curcumin, a polyphenol yellow-orange pigment present in turmeric spices, has a wide range of biological activities, with quite a safety.\u0000\u0000\u0000\u0000This study was aimed to investigate the antioxidant and inhibitory potential against key enzymes involved in human pathology, namely Alzheimer's disease (Acetylcholinesterase (AChE), and Butyrylcholinesterase (BChE)), diabetes (α-glucosidase) and hyperpigmentation and Parkinson’s diseases (Tyrosinase) of curcumin.\u0000\u0000\u0000\u00001,1-diphenyl-2-picrylhydrazyl free radical (DPPH●) and hydrogen peroxide radicals (H2O2) assays were used to evaluate the antioxidant capacity of curcumin, enzyme inhibitory activity was evaluated using in vitro standard procedures.\u0000\u0000\u0000\u0000Curcumin exhibited an excellent antioxidant effect with an IC50 value significantly less than the reference, Vit C. In enzyme inhibitory activity, curcumin demonstrated excellent inhibitory activity against AChE, BChE and α-glucosidase. The finding showed that curcumin was significantly less than the reference galantamine against AChE, but was significantly more than the references galantamine and acarbose against BChE and α-glucosidase, respectively. Whereas for anti-tyrosinase activity, curcumin displayed weak inhibitory activity compared with the standard inhibitor, Kojic acid.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48211169","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, Characterization and Evaluation of 5α, 6β-Dihalo androsterone Derivatives as 5α-Reductase Inhibitors","authors":"Akanksha Sharma, P. Rana, Poonam Arora, T. Kaur, N. Dhingra","doi":"10.2174/1573408018666220525123827","DOIUrl":"https://doi.org/10.2174/1573408018666220525123827","url":null,"abstract":"\u0000\u0000Testosterone under the influence of 5α-reductase enzyme gets converted to dihydrotestosterone and high levels are found to be causative for androgen dependent disease like benign prostatic hyperplasia. Thus, 5α-reductase has been recognised as an important target for discovering new drugs against Benign Prostatic Hyperplasia and Prostate Cancer.\u0000\u0000\u0000\u0000In the present study, a series of 5α, 6β-Dichloro-17-Oxoandrostan-3β-yl esters (7a-7f) were synthesized and characterized by analytical and spectroscopic methods. The compounds were evaluated for their 5α-reductase inhibitory activity in-vivo by their effect on serum androgen level.\u0000\u0000\u0000\u0000The target compounds (7a-7f) showed increased anti-androgenic activity as compared to finasteride and control, which implies that the target compounds are effective in inhibiting 5α-reductase. Particularly, compound 7b showing highest inhibitory activity and noteworthy D-Score was further sorted by performing solubility and dissolution studies. Results of these studies when compared with finasteride showed increased solubility and dissolution of target compound 7b.\u0000\u0000\u0000\u0000These results demonstrated that enhancement of activity by the presence of electronegative group at position 3 of the steroidal nucleus makes 7b a lead compound for further exploration and optimal formulation.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-05-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48370807","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":"L-Proline Catalyzed Knoevenagel Condensation of Aldehydes with Active Methylene Compounds and Their Molecular Modeling Studies for Anti-SARS CoV-2 Potentials","authors":"B. Thorat, Dnyaneshwar T. Nagre, Pawan P Dhurandhar, Pratiksha K. Borase, Sweta Bavkar, Riddhi R. Kasar, Rohan D Narkar, M. Farooqui, Suraj N. Mali","doi":"10.2174/1573408018666220516104525","DOIUrl":"https://doi.org/10.2174/1573408018666220516104525","url":null,"abstract":"\u0000\u0000An efficient one-pot synthesis of 2-alkylidene/arylidene derivatives was reported from active methylene compounds such as malononitrile/ethyl cyanoacetate/5-methyl-2,4-dihydro-3H-pyrazol-3-one and aldehydes in the presence of 10 mol% of L-proline (ethanol at room temperature).\u0000\u0000\u0000\u0000All derivatives were obtained in good to excellent yields. The structures of the synthesized compounds were confirmed from their FTIR (Fourier-transform infrared spectroscopy), 1H-NMR (Proton nuclear magnetic resonance), and mass spectroscopy. The importance of these compounds is predicted from their SAR (structure-activity relationship) study. Moreover, these newer compounds were further docked into various therapeutic targets of the SARS-CoV-2 (severe acute respiratory syndrome–related coronavirus) virus.\u0000\u0000\u0000\u0000Results from our molecular docking suggested that these compounds have good inhibitory properties on the SARS- CoV-2 virus.\u0000\u0000\u0000\u0000L-proline (bifunctional organic catalyst) is found to be the best catalyst for the synthesis of different condensed products from active methylene compounds and aldehydes.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-05-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42883961","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":"Modulation of Prostaglandin E2 with Natural Products for Better Management of Pain and Inflammation","authors":"A. Chopade, Suraj N. Mali","doi":"10.2174/1573408018666220513111051","DOIUrl":"https://doi.org/10.2174/1573408018666220513111051","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":"2022-05-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43537272","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":"Molecular Docking, in vitro Antioxidant, and in vivo Hepatoprotective Activity of Methanolic extract of Calotropis gigantea leaves in Carbon Tetrachloride-induced Liver injury in Rats","authors":"Shripad Bairagi, P. Ghule, R. Gilhotra","doi":"10.2174/1573408018666220511170125","DOIUrl":"https://doi.org/10.2174/1573408018666220511170125","url":null,"abstract":"\u0000\u0000Calotropis gigantea (Asclepiadaceae), a wildly growing plant, has several purported therapeutic characteristics and treats toothache and earache, sprains, anxiety, pain, epilepsy, and mental disorders.\u0000\u0000\u0000\u0000The purpose of this study was to determine the in vitro antioxidant and in vivo hepatoprotective capabilities of a methanolic extract of Calotropis gigantea leaves (CGL) against carbon tetrachloride-induced liver injury in rats.\u0000\u0000\u0000\u0000The Sprague Dawley rats (180-250 g) were used for the current study. The hepatoprotective activity of CGL was determined by estimating the different biochemical parameters like SGOT, SGPT, ALP, bilirubin, and in-vivo antioxidant parameters like LPO, GSH, SOD, and CAT in different animal groups. We have also investigated the inhibitory potential of some significant chemical constituents of CGL on CYP2E1 through molecular docking.\u0000\u0000\u0000\u0000In vivo hepatoprotective studies indicates the CGL extract administration caused a significant reduction [at 200 mg, SGOT (110.16 IU/L), SGPT (101.33 IU/L), ALP (186.66 IU/L), bilirubin (1.1 mg/dl), and LPO (6.933 M/mg protein)] and elevation [GSH (14.051 M/mg protein), SOD (257.5%), and CAT (15.975 μM)] in enzyme activity in a dose-dependent manner. Unfortunately, CGL extract has not shown a more potent activity than the standard drug Silymarin. All the phytoconstituents have shown potent binding affinity with CYP2E1 compared to the native ligand. Amongst all the phytoconstituents, Medioresinol was the most active and potent molecule that has developed compelling interactions with CYP2E1.\u0000\u0000\u0000\u0000From free radical scavenging activity, it was concluded that CGL extract exerts more scavenging activity than ascorbic acid, which indicates a high level of polyphenols and tocopherols and also exhibited in vivo hepatoprotective activity. From the molecular docking, it has been concluded that Calotropis gigantea can potentially inhibit CYP2E1 and prevent the generation of free radicals, which will ultimately reduce oxidative stress and associated diseases.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-05-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46240656","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}