Current Enzyme Inhibition最新文献

{"title":"In Silico Investigation: Opening Doors to Novel Thymidylate Synthase Inhibitors","authors":"Sheenu Mittal, Ankit Gupta, Monika, Richa, R. Chadha, N. Dhingra","doi":"10.2174/1573408016999200602130121","DOIUrl":"https://doi.org/10.2174/1573408016999200602130121","url":null,"abstract":"\u0000\u0000 Lung cancer is presumed to be the most notable cause of morbidity and impermanency\u0000in human beings caused by uncontrolled cell proliferation of lung tissue which results in\u0000abrupt synthesis of DNA.\u0000\u0000\u0000\u0000Prevention of DNA synthesis can show distinctive effect on lung cancer by utilizing Thymidylate\u0000synthase (TS), a key rate-limiting enzyme in the DNA synthesis process. However, the\u0000available finite aggregate of clinically approved blockers and their corresponding side effects lead\u0000to the urgent origination of novel inhibitors.\u0000\u0000\u0000\u0000In silico approaches (QSAR and molecular docking) have been accomplished\u0000to discover new potential inhibitors of TS providing a new strategy to evolve novel thymidylate\u0000synthase inhibitors functional in lung cancer.\u0000\u0000\u0000\u0000In the present study chemical features of a series of compounds alongside their activities\u0000alternating over numerous orders of magnitudes was utilized to generate QSAR models, and these\u0000could be further employed to predict the activity of new designed compounds. 3D‒QSAR kNNSW\u0000based model with decent statistical data having q2 approximately 95% (internal validation) and\u000080% (external validation) has validated the importance of steric feature. Further docking analysis using\u0000D‒score and ligand receptor interactions indicated that all the studied compounds are well accommodated\u0000in the binding pocket of TS and disparities in the activity are controlled by hydrogen\u0000and hydrophobic interactions.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-11-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41362020","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":"The Crystal Structures of Thermomyces (Humicola) Lanuginosa Lipase in Complex with Enzymatic Reactants","authors":"A. McPherson, S. Larson, Andrew Kalasky","doi":"10.2174/1573408016999200511090910","DOIUrl":"https://doi.org/10.2174/1573408016999200511090910","url":null,"abstract":"To understand the details of the action of fungal lipase and the mechanism for its observed interfacial activation. Fungal lipase, crucial to biotechnology, functions at the lipid - water interface where it undergoes a poorly understood interfacial activation. Biochemical factors influencing its activation and inhibition are also poorly understood. This study provides a basis for its activity and a plausible mechanism for interfacial activation. To determine the structures of fungal lipase in different crystal forms in complex with their enzymatic reactants and inhibitors. X-ray crystallography. Thermomyces lanuginosa lipase was visualized in three crystal forms, of space groups H32, P21 and I222 at 1.3 to 1.45 Å resolution. Rhombohedral crystals have one molecule, lacking segment 241 to 252, as an asymmetric unit, with molecules organized as two trimers. Monoclinic crystals’ asymmetric unit is six intact molecules organized as two, nearly identical trimers, each exhibiting an NCS threefold axis. The “lid” helix was consistently closed. Oligomerization into trimers creates an internal hydrophobic cavity where catalysis occurs. In monoclinic and orthorhombic crystals, active site serines were esterified to fatty acids. Lipase had bound within their trimeric, hydrophobic cavities 1,3-diacylglycerols with fatty acid chain lengths of about 18 carbons. Results suggest trimers are likely the active form of the enzyme at the lipid-water interface. Formation of trimers may provide an explanation for “interfacial activation”.","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-11-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46680566","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":"Extracts of Leaves of Six Locally Available Plants from Bagmati Province of Nepal as Potent Inhibitors of Alpha-amylase, Lipase, Tyrosinase, Elastase, and Cholinesterases","authors":"B. Pandey, S. Pradhan, K. Adhikari, Prayon Joshi, S. Malla","doi":"10.2174/1573408016999200624150750","DOIUrl":"https://doi.org/10.2174/1573408016999200624150750","url":null,"abstract":"\u0000\u0000Medicinal plants and their products are gaining global popularity due to\u0000their several health benefits. However, the biological activities of the vast majority of medicinal plant\u0000species have not been explored yet. In this study, we evaluated the enzyme inhibitory potential of six\u0000medicinal plant species involved in digestion, skin-related problems, and neurological problems.\u0000\u0000\u0000\u0000The 80% methanol extracts of leaves of six locally available plants from the Bagmati province\u0000of Nepal were analyzed for their flavonoids content, phenolics content, antioxidant activity, and\u0000enzymes inhibitory potential. Antioxidant activity was analyzed by the DPPH assay. Alpha-amylase\u0000inhibition was carried out by the DNSA method. Lipase, tyrosinase, elastase, acetylcholinesterase,\u0000and butyrylcholinesterase inhibitions were analyzed by using p-NPB, L-DOPA, AAAPVN,\u0000acetylthiocholine, and butyrylthiocholine as a respective substrate.\u0000\u0000\u0000\u0000Among the analyzed plants species, Artocarpus heterophyllus displayed highest α-amylase\u0000(IC50=6.28 ± 0.01 μg/mL), lipase (IC50= 475.14 ± 3.17 μg/mL), elastase (IC50= 72.75 ± 3.41 μg/mL)\u0000and acetylcholinesterase (IC50= 68.66 ± 1.71 μg/mL) inhibition, whereas, Actinidia deliciosa displayed\u0000highest tyrosinase inhibition (IC50=139.87 ± 0.72 μg/mL) and butyrylcholinesterase inhibition\u0000(IC50= 18.32 ± 0.44 μg/mL). Furthermore, Jasminum humile showed no inhibitory tendencies against\u0000elastase and Lygodium japonicum showed no inhibition towards lipase and elastase at the given concentration\u0000range.\u0000\u0000\u0000\u0000Our study revealed that A. deliciosa and A. heterophyllus are the potential source of α-\u0000amylase, lipase, elastase, acetylcholinesterase, and butyrylcholinesterase inhibitors. Based on our\u0000findings, we concluded that the analyzed plant species are of great scientific interest to the pharmaceutical,\u0000cosmetics, and food industries.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-11-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42502309","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":"Insight into the Mechanism of 17β-Hydroxysteroid Dehydrogenase Type 3 Inhibition by the Androsterone Derivative RM-532-105","authors":"P. Stephen, J. Roy, R. Maltais, D. Poirier","doi":"10.2174/1573408016999200729110245","DOIUrl":"https://doi.org/10.2174/1573408016999200729110245","url":null,"abstract":"\u0000\u0000The last step in the production of androgen testosterone from 4-androstene-\u00003,17-dione (4-dione) in testis involves the 17β-hydroxysteroid dehydrogenase type 3 (17β-HSD3).\u0000Blocking this microsomal enzyme with an inhibitor would lower the level of testosterone and, consequently,\u0000could be an approach for the treatment of androgen-dependent diseases. RM-532-105 was\u0000developed as a steroidal inhibitor of 17β-HSD3, but its mechanism of action is not yet known.\u0000\u0000\u0000\u0000To identify potential binding sites of the 17β-HSD3 substrate 4-dione, cofactor NADPH,\u0000as well as inhibitor RM-532-105.\u0000\u0000\u0000\u0000Since there is no crystal structure of 17β-HSD3 available, complexed or not with a ligand,\u0000a homology model was prepared followed by molecular docking, and enzymatic assay experiments\u0000were performed.\u0000\u0000\u0000\u0000Transfected LNCaP prostate cancer cells were used as a source of 17β-HSD3 activity for the\u0000transformation of 4-dione into testosterone in the presence of varying concentrations of a substrate, a\u0000cofactor or an inhibitor. Molecular modeling experiments and enzymatic assays with these cells suggest\u0000a competitive action of RM-532-105 with the cofactor and a non-competitive action with the\u0000substrate 4-dione.\u0000\u0000\u0000\u0000These results allow the selection of one inhibitor orientation in the enzyme binding site,\u0000from the two possibilities predicted by the docking experiments, and appear to be in agreement with\u0000previous structure-activity relationships.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-11-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41330957","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":"The Role of STAT3 Signaling in Different Types of Cancers: A Comprehensive Review","authors":"Kaviarasan Lakshmanan, Gowramma Byran, S. Bandlamudi, P. Krishnamurthy","doi":"10.2174/1573408016999200708160300","DOIUrl":"https://doi.org/10.2174/1573408016999200708160300","url":null,"abstract":"\u0000\u0000Signal transducer and activator of transcription (STAT3) is an important transcription factor\u0000capable of mediating or even driving cancer progression through hyperactivation or gain-offunction\u0000mutations. It plays a key role in regulating host immune and inflammatory responses and in\u0000the pathogenesis of many cancers. However, compelling evidence suggests that STAT3 is constitutively\u0000activated in many cancers and plays a vital role in tumor growth and metastasis. Hyperactive\u0000STAT3 is also implicated in various hematopoietic and solid malignancies, such as chronic and acute\u0000myeloid leukemia, melanoma or prostate cancer. The classical understanding of STAT functions is\u0000linked to their phosphorylated parallel dimer conformation, in which they induce gene transcription.\u0000In this review, we discuss the functions and the roles of STAT3 signal in various types of cancers.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-11-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45868244","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":"Unprecedented Role of the N73-F124 Pair in the Staphylococcus equorum MnSOD Activity","authors":"D. Retnoningrum, H. Yoshida, M. D. Razani, V. F. Meidianto, A. Hartanto, A. Artarini, W. Ismaya","doi":"10.2174/1573408016999201027212952","DOIUrl":"https://doi.org/10.2174/1573408016999201027212952","url":null,"abstract":"\u0000\u0000Bacterial manganese superoxide dismutase (MnSOD) occurs as a dimer,\u0000which is responsible for its activity and stability. Therefore, increasing the dimeric strength would increase\u0000the stability of the enzyme while maintaining its activity.\u0000\u0000\u0000\u0000An N73F substitution was introduced to strengthen interactions between the monomers at\u0000the dimer interface. This substitution would introduce a π-stacking interaction between F73 of one\u0000monomer to F124 from the other monomers.\u0000\u0000\u0000\u0000Site-directed mutagenesis was carried out to substitute N73 with phenylalanine. The activity\u0000of the mutant was qualitative- and quantitatively checked while the stability was evaluated with a fluorescence-\u0000based thermal-shift assay. Finally, the structure of the mutant was elucidated by means of Xray\u0000crystallography.\u0000\u0000\u0000\u0000The N73F mutant activity was only ~40% of the wild type. The N73F mutant showed one TM\u0000at 60+1°C while the wild type has two (at 52-55°C and 63-67°C). The crystal structure of the mutant\u0000showed the interactions between F73 from one monomer to F124 from the other monomer. The N73F\u0000structure presents an enigma because of no change in the enzyme structure including the active site.\u0000Furthermore, N73 and F124 position and interaction are conserved in human MnSOD but with a different\u0000location in the amino acid sequence. N73 has a role in the enzyme activity, likely related to its interaction\u0000with F124, which resides in the active site region but has not been considered to participate in\u0000the reaction.\u0000\u0000\u0000\u0000The N73F substitution has revealed the unprecedented role of the N73-F124 pair in the\u0000enzyme activity.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-10-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48175257","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":"Relationship with Metalloproteinase 13, E-cadherin, Homocysteine and Co Factors Folic Acid and Vitamin B12 in Patients Diagnosed with Prostate Cancer","authors":"T. Gascón, Beatriz G. Lourenço, E. Pereira, Beatriz A. da Costa Aguiar, G. L. Veiga, Flávia de Sousa Gehrke, F. Adami, F. Fonseca","doi":"10.2174/1573408016999201026195354","DOIUrl":"https://doi.org/10.2174/1573408016999201026195354","url":null,"abstract":"\u0000\u0000 Prostate cancer (Pc) is the most frequent neoplasia in men and the second\u0000cause of death in Brazil.\u0000\u0000\u0000\u0000To analyze the interactions and biologicals responses of Pc oxidative stress and prostatespecific\u0000antigen (PSA), E-cadherin and MMP-13. Demonstrate whether the increase of the amount of\u0000the form of E-cadherin found in the plasma of Pc patients, correlates with decrease of the PSA.\u0000\u0000\u0000\u0000Samples were obtained through peripheral venipuncture to analyse parameters of biomarkers\u0000pc as PSA, E-cadherin, MMP-13, Homocysteine, Folic acid, Vitamin B12, Testosterone T and free following\u0000the patients diagnosis, 3 and 6 months during their treatment to analyze the biological responses\u0000of Pc oxidative stress.\u0000\u0000\u0000\u0000 The analysis was performed by using immunoenzymatic assay. Statistical data processed\u0000through Excel in Windows Vista and analyzed through the Shapiro-wilk Test, ANOVA, and Spearman\u0000Test. An increase in the concentration of E-cadherin (p = 0.02), as a decrease in concentration of PSA\u0000(p < 0.001), total testosterone (p < 0.001) and free testosterone (p = 0.02) was observed during the\u0000treatment period without significant alterations in the remaining markers for either of the periods.\u0000\u0000\u0000\u0000It was found that during treatment of men diagnosed with pc that there was an an increase\u0000in the concentration of plasmatic E-cadherin, which was negatively correlated with the concentrations\u0000of folic acid (-0,03 (0,87) rs (p). It was observed that the levels of hcy are positively correlated with\u0000concentrations of total testosterone and a negative correlation. Vitamins B12 remained within the parameters\u0000of normality during the entire study.\u0000\u0000\u0000\u0000P.S.A levels were free and total testosterone levels decreased. In this way, monitoring the\u0000folic acid, E-cadherin dosages of patients during the treatment phases can effectively complement in the\u0000face of remission, since it would be a way of preventing abnormal cell replications, with a clinical view\u0000prudent so that the cell methylation cycle is not affected.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-10-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42485940","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 and In vivo Effects of 17β-N-(4-phenylcarbamoyl) androst-4-en-3- one Derivatives as 5a-reductase Inhibitors on Androgen-dependent Glands","authors":"M. Cabeza, Lucero Bautista, E. Bratoeff, Juan Soriano, Y. Heuze","doi":"10.2174/1573408016999200928153524","DOIUrl":"https://doi.org/10.2174/1573408016999200928153524","url":null,"abstract":"\u0000\u00005α-reductase inhibitors have been proven useful for the treatment of prostate\u0000diseases, which can be due to the unregulated activity of 5α-reductase enzyme. This study was focused\u0000on determining the activity of four different derivatives of 17β-phenyl carbamoyl-androst-4-en-3-one\u00001–4 as inhibitors of 5α-reductase (5RD5A), to improve the effects of current drugs.\u0000\u0000\u0000\u0000In vitro effect of compounds 1-4 on the activity of the human prostate enzyme, 5α-reductase,\u0000was determined by measuring IC50 values, the concentration of a compound that inhibits the activity of\u00005RD5A2 by 50%. In vivo, the pharmacological effects of compounds 1-4 were identified in a hamster\u0000model of prostate hypertrophy.\u0000\u0000\u0000\u0000The steroidal 17β-carboxamides 1, 3, and 4 (IC50 = 5±0.5, 0.112±0.045, 0.167±0.056 nM) significantly\u0000inhibited the in vitro activity of the 5RD5A2 enzyme with higher potency than finasteride,\u0000which is a drug known as a specific 5RD5A2 inhibitor (IC50 = 8.5±0.3 nM). Compounds 1, 3, and 4\u0000were more potent than finasteride to decrease the size of hamster flank organs in castrated animals\u0000treated with testosterone. Also, compounds 1-4 were more effective than finasteride itself to reduce the\u0000weight of the prostate in the hamster model, without producing toxicological effects during the six days\u0000of treatment.\u0000\u0000\u0000\u0000 In conclusion, the steroidal 17 β-carboxamides 1-4 were suitable inhibitors of human\u00005RD5A2 activity, in addition to being able to reduce prostate weight without causing toxicity. These\u0000steroids could, therefore, have promising therapeutic potential for the treatment of benign prostatic hyperplasia.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-09-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42199769","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":"Investigation of the Effect of Loratadine and Calcium Ions on Oxidoreductase Activity of Catalase Enzyme","authors":"E. Hasković, S. Herenda, Zehra Halilović, S. Unčanin, Denis Hasković, Ena Deljkić","doi":"10.2174/1573408016999200817173859","DOIUrl":"https://doi.org/10.2174/1573408016999200817173859","url":null,"abstract":"\u0000\u0000The Spectrophotometric method is one of the most suitable analytical techniques\u0000for testing the activity of enzymes under the influence of various factors.\u0000\u0000\u0000\u0000The effect of H1-antihistamines of loratadine and calcium ions on enzyme catalase under\u0000in vitro conditions was investigated in this paper.\u0000\u0000\u0000\u0000 It has been shown that loratadine is a partial inhibitor of catalase, but this\u0000effect is diminished in the presence of calcium ions. Calcium as well as other cations are important\u0000for many biological and cellular functions. The kidneys play a central role in the homeostasis of these\u0000ions. The activity of the catalase enzyme under the given conditions, the type of inhibition, and the\u0000kinetic parameters of the enzyme reaction were determined.\u0000\u0000\u0000\u0000We concluded that loratadine is a partially competitive inhibitor.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-08-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43483623","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":"Lactobacillus Rhamnosus UBLR-58 and Diclofenac Potentiate the Anti- Alzheimer Activity of Curcumin in Mice","authors":"Sonali Pande, C. Patel, D. Sarkar, S. Acharya","doi":"10.2174/1573408016999200817170821","DOIUrl":"https://doi.org/10.2174/1573408016999200817170821","url":null,"abstract":"\u0000\u0000 Curcumin, a providential spice, has its role in protecting the brain from neurodegeneration.\u0000Despite its ubiquitous role, it is not exploited alone due to its hampered bioavailability.\u0000By restraining the intestinal and liver enzymatic metabolism, one can boost the bioavailability of\u0000curcumin and promotes reabsorption of the curcumin. Diclofenac inhibits uridine 5'-diphosphoglucuronosyltransferase\u0000enzymes specifically responsible for the metabolism and elimination of curcumin.\u0000Lactobacillus rhamnosus is able to synthesize and release the β -d-glucuronidase enzyme,\u0000which reverts curcumin into the active form.\u0000\u0000\u0000\u0000In this research, we aim to combine curcumin with Lactobacillus rhamnosus and diclofenac\u0000as an adjuvant with curcumin to potentiate anti-Alzheimer effect in mice impaired with\u0000memory by scopolamine.\u0000\u0000\u0000\u0000To induce amnesia, scopolamine was used in mice model (1mg/kg, daily for 10 days i.p.).\u0000After execution of behavioural tests (Morris Water Maze test), brain and liver were isolated for further\u0000neurochemical and histopathology examination.\u0000\u0000\u0000\u0000Our finding showed a marked rise in the level of antioxidant enzymes in curcumin with L.\u0000rhamnosus and diclofenac compared to curcumin alone. Additionally, the behavioural study revealed\u0000that cognition in mice with curcumin adjuvant with L. rhamnosus and diclofenac showed a marked\u0000improvement. The histology study proves that curcumin alone possesses less and a non-significant\u0000neuroprotective effect as compared to curcumin with L. rhamnosus and diclofenac.\u0000\u0000\u0000\u0000 This entire outcome ratifies that curcumin with L. rhamnosus and diclofenac has higher\u0000activity as compared to curcumin alone, which reversed the cognition in the Alzheimer disease model.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-08-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43380745","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}