Current Enzyme Inhibition最新文献

{"title":"In-silico Exploration of Phytoconstituents of Gymnema sylvestre as Potential Glucokinase Activators and DPP-IV Inhibitors for the future Synthesis of Silver Nanoparticles for the Treatment of Type 2 Diabetes Mellitus","authors":"A. B. Chavan, K. Daniel, A. Patel","doi":"10.2174/1573408017666211029160203","DOIUrl":"https://doi.org/10.2174/1573408017666211029160203","url":null,"abstract":"\u0000\u0000Diabetes has a large death toll worldwide, particularly as it falls into the ten leading causes of death. Type 2 diabetes mellitus (T2DM) occurs as the body becomes resistant to insulin and sugar accumulates in the blood. It has been observed that, dipeptidyl peptidase-IV (DPP-IV) inhibitors and glucokinase activators are known therapeutic agents to treat T2DM. Among the possible medicinal plants, Gymnema sylvestre (GyS) belongs to the Apocynaceae family and is traditionally used for the treatment of different diseases. This plant is also known as 'Gurmur' because it has a sugar reducing ability. GyS was known to be one of the main botanicals for the treatment of diabetes. \u0000\u0000\u0000\u0000\u0000Rendering to the studies described above, we have tried to investigate the natural DPP-IV inhibitors and potent glucokinase activators from the phytoconstituents of GyS. New drug candidates from the medicinal plant GyS have been reported as potent DPP-IV inhibitors and glucokinase activators. \u0000\u0000\u0000\u0000\u0000As a preliminary investigation, we have studied the effectiveness of phytoconstituents of GyS in T2DM through molecular docking as a proof of concept of synthesizing silver nanoparticles (for the treatment of T2DM) using extract of this plant. \u0000\u0000\u0000\u0000\u0000 The present investigative research showed that diabetes mellitus has important values in the recognized compounds included in the present analysis. The nine compounds selected were evaluated on the basis of DPP-IV and glucokinase enzyme binding energy values and their drug properties. Except quercitol, all the selected compounds have exhibited very potent glucokinase activation potential than its native ligand. Gymnemasin A, lupeol, gymnemoside A, gymnemasaponin V and gymnemic acid I have shown excellent DPP-IV inhibitory potential. \u0000\u0000\u0000\u0000\u0000 We are aiming to synthesis the silver nanoparticles of leaf extract of GyS for the treatment of T2DM. As a preliminary investigation, we have studied the effectiveness of phytoconstituents of GyS in T2DM through molecular docking as a proof of concept of synthesizing silver nanoparticles (for the treatment of T2DM) using extract of this plant. As a result of present investigation, it has been concluded that these compounds can be used to treat the T2DM and hence in future we will synthesize the silver nanoparticles of GyS extract for the treatment of T2DM.\u0000\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2021-10-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42294324","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 inhibitory Effects of Some Artificial Food Colorings on α-amylase and α-glucosidase: In Vitro and In Silico Studies","authors":"Reguia Mahfoudi, A. Djeridane, D. Tahri, M. Yousfi","doi":"10.2174/1573408017666211018102605","DOIUrl":"https://doi.org/10.2174/1573408017666211018102605","url":null,"abstract":"\u0000\u0000 Inhibition of α-amylase and α-glucosidase is considered as an important therapeutic target to manage type 2 diabetes mellitus (T2DM), reducing postprandial hyperglycemia (PPHG).\u0000\u0000\u0000\u0000\u0000The present work explored the antidiabetic activities of five artificial food colorings by α-amylase and α-glucosidase enzyme inhibition in vitro and in Silico.\u0000\u0000\u0000\u0000\u0000 In this study, inhibition of α-amylase and α-glucosidase were evaluated. Further, the interaction between enzymes (α-amylase and α-glucosidase) and ligands (food colorings) was followed by QSAR and molecular docking studies. \u0000\u0000\u0000\u0000\u0000 The in vitro results obtained show that the blue patent (SIN131) exhibited more potent inhibition with IC50 values of 0.03± 0.01 mM and 0.014±0.001 mM against α-amylase and α-glucosidase inhibition respectively compared to acarbose. The QSAR study found a strong correlation between IC50 values with four molecular descriptors. This linear regression confirms that a strong polarity (Apol) and a low hydrophobia (ALogP) favor the inhibitory effect of these colorings toward both enzymes. Also, a negative role of the number of heavy atoms has been demonstrated in the phenomenon of inhibition of this enzyme. Finally, the descriptor εlumo (electronic affinity) plays a crucial role on the inhibitory power of these dyes toward both enzymes by electron transfer. The virtual screening of the inhibition of α-amylase and α-glucosidase by these colorings, using Molegro Virtual Docker (MVD), allowed us to obtain stable complexes with interaction energies resulting from the place of hydrogen bonds and several hydrophobic interactions. However, the sulfonate groups of these colorings can be the major factors in the inhibition of these enzymes. On the other hand, Rerank Score with the pose are perfectly correlated (R2> 0.76) to the inhibitory activity of these food colorings measured experimentally. \u0000\u0000\u0000\u0000\u0000The present study suggests that the Blue Patent V (SIN131) effectively act as α-amylase and α-glucosidase inhibitor leading to a reduction in starch hydrolysis and hence eventually to lowered glucose levels.\u0000\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2021-10-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44508829","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":"Targeting histidine for developing a new generation of covalent enzyme inhibitors","authors":"D. Poirier","doi":"10.2174/1573408017666211008141335","DOIUrl":"https://doi.org/10.2174/1573408017666211008141335","url":null,"abstract":"\u0000\u0000Despite the significant number of irreversible inhibitors developed over the years, strong prejudices remain for this type of therapeutic molecule, particularly in the area of drug development. New generations of covalent targeted inhibitors are, however, in development, and interest is increasingly growing. In fact, the new generation of covalent inhibitors has a weakly reactive species (warhead) that is able, in a particular context, to selectively form a chemical bond with a given amino acid residue, which can be irreversible or reversible. In addition to new selective warheads, new amino acids are also targeted. In the following text, we will focus on covalent targeted inhibitors that selectively alkylate histidine.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2021-10-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47299613","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":"Experimental and Computational Insights into Bis-indolylmethane Derivatives as Potent Antimicrobial Agents Inhibiting 2,2-dialkylglycine Decarboxylase","authors":"Dnyaneshwar T. Nagre, B. Thorat, Suraj N. Mali, M. Farooqui, B. Agrawal","doi":"10.2174/1573408017666210914105731","DOIUrl":"https://doi.org/10.2174/1573408017666210914105731","url":null,"abstract":"\u0000\u0000A series of bis(indolyl)methanes (3a-3o) have been synthesized using a greener and new approach using the reaction of different substituted aldehydes and indole in the presence of an easily available and biodegradable base such as piperidine in acetic acid at room temperature and characterized with UV (Ultraviolet-visible spectroscopy), Gas chromatography-mass spectrometry (GC-MS), Proton nuclear magnetic resonance (H-NMR), and Fourier transform infrared spectroscopy (FTIR). \u0000\u0000\u0000\u0000\u0000All 15 newly synthesized compounds (3a-3o) were subjected to in-vitro anti-microbial activity determination and compared with the known standard drug ciprofloxacin (1-2 µg/mL). Our in-silico analysis on the target protein, pdb id: 1d7u suggested that these analogues would be highly active against bacterial targets and thus, would act as good antimicrobial agents. \u0000\u0000\u0000\u0000\u0000All 15 newly synthesized compounds (3a-3o) displayed potent activity on various experimental microbial strains (1.0-1.4 µg/mL). Compound, 3k was obtained as the best docked compound against common bacterial target enzyme, (pdb id:1d7u). The standard, Ciprofloxacin, retained the docking score of -111.3 Kcal/mol with similar binding amino acid residues (LYS272 (Pi-cation); ALA A:245 (Pi-sigma); TRP A:138 (Pi-Pi); ALA A:112; and MET A:141 (Pi-alkyl)) as of inbound.\u0000\u0000\u0000\u0000\u0000We believe that our current study would shed more light on the development of potent bis(indolyl)methanes as antimicrobial agents.\u0000\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2021-09-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46728442","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 N224 glycosylation in Saccharomycopsis fibuligera R64 α-amylase on enzyme activity and stability","authors":"Yovin Sugijo, T. D. Rosahdi, Fernita Puspasari, W. Ismaya, Khomaini Hasan, Ihsanawati, T. Subroto, D. Natalia","doi":"10.2174/1573408017666210809111830","DOIUrl":"https://doi.org/10.2174/1573408017666210809111830","url":null,"abstract":"\u0000\u0000The amino acid sequence of an α-amylase of the yeast Saccharomycopsis fibuligera R64 (SfamyR64) contains the two putative N-linked glycosylation sites N153 and N224. N224 is hypothetically responsible for the binding of starch substrate because it is highly conserved among SfamyR64 homologs. \u0000\u0000\u0000\u0000To test whether N224 plays a key role in enzyme activity and stability. \u0000\u0000\u0000\u0000N224Q substitution was introduced by site-directed mutagenesis. The wild type and the mutant were independently over-produced in Pichia pastoris KM71. Activity of the wild type and of the mutant were compared, and their thermal-stability was assessed using heat treatments. The evolutionary relationship of SfamyR64 with its structural homologs with different glycosylation patterns was examined. \u0000\u0000\u0000\u0000Activity of the N224Q mutant was approximately 80% lower than that of the wild type. The mutant showed no activity after 10 min of pre-incubation at 50 °C, whereas the wild type SfamyR64 showed activity until 30 min of treatment. Sfamy appeared to have evolved earlier than its structural homolog.\u0000\u0000\u0000\u0000SfamyR64 N224 is crucial for enzyme activity and thermal stability. This glycosylation site is unique for fungal and bacterial α-amylases.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2021-08-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47730563","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":"Biological characterization and preliminary crystallization: A step towards the use of Novel Allium sativum Protease inhibitor as a potential therapeutic drug","authors":"Tooba Naz Shamsi, Sumbul Afreen, Romana Parveen, Manish Kumar, T. Fatma, S. Fatima","doi":"10.2174/1573408017666210809104744","DOIUrl":"https://doi.org/10.2174/1573408017666210809104744","url":null,"abstract":"\u0000\u0000Garlic, being a well-known medicinal plant is the most commonly used culinary spice worldwide. Investigation of protease inhibitor isolated from garlic leads to a promising contender in pharmacognostic and pharmacological studies.\u0000\u0000\u0000\u0000Protease Inhibitor (PI) from 'garlic' (Allium sativum) was analyzed for its biological role as an antioxidant, antimicrobial, and anti-inflammatory agent. \u0000\u0000\u0000\u0000Antioxidant activity was evaluated using ferric ion reducing antioxidant power (FRAP) and 2, 2-diphenyl-1-picrylhydrazyl (DPPH) assays. The anti-inflammatory activity was assessed using trypsin inhibitory assay and heat-induced albumin denaturation method. The antimicrobial activity was examined in broth against E. coli and B. Subtilis. The crystallization was setup using the hanging drop method.\u0000\u0000\u0000\u0000ASPI showed DPPH radical scavenging with IC50 values 561±0.337 µg/ml. Also, ASPI showed the highest value of 0.699±0.009 mM at 1000 μg/ml and the lowest i.e. 0.181±0.006 mM at 100 μg/ml in FRAP assay. Ascorbic acid was taken as standard in both cases. ASPI showed IC50 values of 651±0.532 μg/ml and ~657±1.802 μg/ml respectively. The antibacterial role of ASPI was testified and results showed maximum inhibition against E. coli (ATCC 25922) i.e., 87.8 ±0.602% but no inhibition against B. subtilis (MTCC 736). Cuboidal shaped crystals of the ASPI were obtained in 4-6 weeks using 0.2M calcium chloride dihydrate, 0.1M sodium acetate trihydrate, 20 % isopropanol.\u0000\u0000\u0000\u0000ASPI has tremendous potential for the development of suitable drugs in pharmaceutical industries against diseases due to the generation of reactive oxygen species and cancer. The cuboidal crystals were obtained which is the first study in the context of crystallization of ASPI to date.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2021-08-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48524487","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":"Isolation of Actinomycetes and Screening for Lipase Inhibitors Production","authors":"Shivabai Chandwad, Chandrasen Chandwad, S. Gutte","doi":"10.2174/1573408017666210728141245","DOIUrl":"https://doi.org/10.2174/1573408017666210728141245","url":null,"abstract":"\u0000\u0000Background: Obesity is a growing global health problem. Obesity leads to cardiovascular disorders, musculoskeletal disorders, diabetes, and certain types of cancer. One of the approach to control and treatment of obesity has involved inhibition of dietary lipid digestion by pancreatic lipase inhibitors. Microbes and plant source provide a rich source of enzyme inhibitors including pancreatic lipase inhibitors that can be developed as a drug for obesity treatment.\u0000\u0000Objective: Objective of the work mainly focuses and highlights on the isolation of actinomycetes and screening for pancreatic lipase inhibitors production. \u0000\u0000Methods: Actinomycetes were isolated from soil samples by pre-treatment of samples and using selective growth medium with and without antibiotics. Isolated actinomycetes were grown in fermentation condition and metabolites were extracted with isopropyl alcohol and solvent evaporated to get crude material. Extract of each isolate screened for pancreatic lipase inhibition using p- nitrophenyl palmitate as substrate by spectroscopic method.\u0000\u0000Results: Total 86 actinomycetes strains were isolated from soil samples. Out of 86 extracts,10 extracts have shown positive results for porcine pancreatic lipase inhibition and inhibition activity was in the range of 10-80%. 50 % inhibitory concentration determined using 1 to 8 mg/mL extract in the assay. Extract of isolate A9, B3 and C6 having 50 % inhibitory activity below 3 mg/mL concentration and Orlistat as a standard has shown 50 % inhibitory activity at below 1 mg/mL concentration.\u0000\u0000Conclusion: The results conclude that actinomycetes are potential source of lipase inhibitors, which may lead to valuable novel drugs for obesity treatment.\u0000\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2021-07-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48859805","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":"Potential inhibitor of adenylyl sulfate reductase isolated from Desulfovibrio desulfuricans with PU/PU-Ag to control pitting corrosion of oil tanks and pipelines.","authors":"Wafaa A. Koush, A. Labena, Hany Elsawy, L. Farahat, Tarek M. Mohamed, Maha M. Salem","doi":"10.2174/1573408017666210705123927","DOIUrl":"https://doi.org/10.2174/1573408017666210705123927","url":null,"abstract":"This study aims to alleviate the microbiologically affected corrosion that occurred by sulfate-reducing bacteria (SRB) through synthesizing a bio-based polyurethane polymer and its nanocomposite coating, silver nanoparticles (PU-Ag). Moreover, this study aims to evaluate the effect of PU alone and PU-Ag as inhibitors for adenylyl sulfate reductase (APS), which is the main enzyme for sulfate reduction.\u0000\u0000\u0000\u0000\u0000 In this study, the PU was prepared from the vegetable soybean oil, and the silver nanoparticles (Ag-NPs) with a concentration of 1% were coated to the PU, forming a nanocomposite. The PU and the PU-Ag were characterized and evaluated as inhibitors of the APS reductase enzyme.\u0000\u0000\u0000\u0000\u0000 The results obtained from FTIR, UV, DLS, TEM, and XRD confirmed the preparation structure of the PU and PU-Ag. Furthermore, the PU/PU-Ag competitively inhibited the APS reductase with an inhibition constant equal to 35.7 and 11 mg, respectively. These indicated the exert inhibitory effect of PU/PU-Ag upon the activity of the APS reductase enzyme.\u0000\u0000\u0000\u0000\u0000 The APS reductase enzyme produced by SRB, which is recorded as a big problem in the oil and gas industry, such as pitting corrosion of tanks and pipelines, could be inhibited by PU and PU-Ag.","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2021-07-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47276381","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 Antioxidant, α-amylase and Horseradish Peroxidase Inhibitory Potential of Phenolics Extracts from Chamomilla pubescens, Pulicaria crispa and Rhanterium adpressum growing in Algeria","authors":"Feriel Mahfoudi, M. Reguia, M. Harrat, A. Djeridane, M. Yousfi","doi":"10.2174/1573408017666210506154339","DOIUrl":"https://doi.org/10.2174/1573408017666210506154339","url":null,"abstract":"\u0000\u0000Plants are a main source of drugs for the therapy of a large number of diseases. \u0000\u0000\u0000\u0000The aim of the present work is to evaluate the in vitro antioxidant and anti-α-amylase and anti-peroxidases (HPR) potentials of phenolic extracts obtained from three spontaneous plants; growing in the South of Algeria such as (Chamomilla pubescens, Pulicaria crispa, and Rhanterium adpressum). This is the first report on the study of α-amylase and horseradish peroxidase (HRP) inhibitory activity for phenolic extracts from the Chamomilla pubescens and Pulicaria crispa plants. \u0000\u0000\u0000\u0000The antioxidant activity was evaluated in vitro using four tests: DPPH, CUPRAC, FRAP, and ABTS. The phenolic, flavonoid, and tannin compounds of the three selected Algerian plants were quantified. Also, the inhibition of α-amylase and HRP was evaluated. \u0000\u0000\u0000\u0000The quantification of the total phenolic contents revealed that they are widely variable, and depending on extraction solvents, the highest content was recorded by the ethyl acetate extract of Chamomilla pubescens (flowers) 774.93±60.14mg/100 g of dry matter. In all the antioxidant tests, ethyl acetate extracts showed the most effective activity, which the best was (VCEAC = 65.62 ±0.50 µM/g dry matter) of Pulicaria crispa for the DPPH test. Furthermore, the results of α-amylase and peroxidase inhibitory effects indicated that all plants extracts have inhibitory effects on the two enzymes, with AEIC values ranged from 76.55±3.54 to 149.54±6.68 μM/g of dry matter for the α-amylase, and CEIC values ranged from 8.89±2.22 to 9668.31±254.42 μM/g of dry matter for the peroxidase (HRP). \u0000\u0000\u0000\u0000The present study results suggest that the three Algerian spontaneous plant species (Rhanterium adpressum, Pulicaria crispa, and Chamomilla pubescens) inhibit peroxidase and α-amylase and exhibit a high antioxidant activity what can be related to the treatment of diabetes and thyroid diseases. \u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2021-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42192999","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":"Strong antihemolytic and antioxidant properties of aqueous extract from Algerian Hammada elegans (Bge.) Botsch (Chenopodiaceae)","authors":"Brahim Asseli, Reguia Mahfoudi, A. Djeridane, M. Yousfi","doi":"10.2174/1573408017666210419115739","DOIUrl":"https://doi.org/10.2174/1573408017666210419115739","url":null,"abstract":"\u0000\u0000Research on medicinal plant antioxidants has emerged as a potential therapeutic to prevent free radical generated damage in the human body. Hammada elegans Botsch (popularly known as “Ajram”) is a xerophytic plant widely found in Laghouat region, but there are only a few reports about the biological or chemical properties of these species. Hence, the aim of this study is to investigate the antioxidant and the antihemolytic activities of hexanic, acetonic, methanolic and aqueous extracts of aerial parts of Algerian Hammada elegans Botsch by employing different in vitro assay systems. \u0000\u0000\u0000\u0000 The total phenolic content, the flavonoid content and the condensed tannin amount were analyzed using Folin-Ciocalteu, aluminum chloride and vanillin assays, respectively. The in vitro antioxidant capacity of extracts was assessed by CUPRAC, iron chelating, ABTS•+and antihemolytic assays, and was expressed as EC50 values.\u0000\u0000\u0000\u0000Among the analyzed extracts, the aqueous extract had the highest phenolic, flavonoid and tannin contents. Also, this extract displayed the highest antioxidant capacities compared to the other extracts and standards. Its EC50 value for ABTS radical-scavenging activity was 0.265 ± 0.003 mg/L. Moreover, this extract showed high iron (II) chelating ability (EC50 = 0.958 ± 0.001 mg/L), and good antioxidant activity in the cupric ion reducing activity (CUPRAC) in a concentration dependent manner (EC50 were 0.709 ± 0.002 mg/L). Additionally, this extract had the best antihemolytic activity against AAPH-induced hemolysis (EC50=0.090 ± 0.004 mg/L). \u0000\u0000\u0000\u0000Our study revealed that the aqueous extract of Hammada elegans Botsch, is a potential source of antioxidants which possess a high protective effect of membrane against free radical.\u0000\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2021-04-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47157522","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}