Nesrine Sadaoui-Smadhi, S. Khemili-Talbi, Wadood Abdul, S. Toubal, W. Mokhtari, N. Benhabyles, K. Arab, Khettal Bachra, R. Fazal
{"title":"阿尔及利亚白毛杉精油主要成分紫苏醛和d -柠檬烯对硅胆碱酯酶和单胺氧化酶抑制活性的研究","authors":"Nesrine Sadaoui-Smadhi, S. Khemili-Talbi, Wadood Abdul, S. Toubal, W. Mokhtari, N. Benhabyles, K. Arab, Khettal Bachra, R. Fazal","doi":"10.3844/ajbsp.2019.42.45","DOIUrl":null,"url":null,"abstract":"In a continuation of our previous work for the exploration of novel enzyme inhibitors, molecular modeling was used to inspect the binding mode of perillaldehyde and D-limonene, the major compounds of essential oil of Algerian Ammodaucus leucotrichus into the active site pocket of cholinesterase (AChE and BuChE) and Monoamine Oxidase (MAO). The molecular docking was carried out using Molecular Operating Environment (MOE) software package. Docking analysis showed that this compounds (perilladehyde and D-limonene) can interact with both the Catalytic Active Site (CAS) of AChE, BuChE and MAO. For D-limonene, molecular docking showed favorable H-phi interaction with catalytic residue of AchE and BuChE. The perillaldehyde showed best interaction profile with BuChE as compared with compound D-Limonene. The best interaction between perilladehyde and monoamine oxidase was also revealed. This paper shows best correlation between the in vitro study and the in silico molecular docking study of anti-cholinesterase and anti-monoamine oxidase activities.","PeriodicalId":11025,"journal":{"name":"Current Research in Bioinformatics","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2019-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"In Silico Cholinesterase and Monoamine Oxidase Inhibitory Activities of Perillaldehyde and D-Limonene, Main Compounds of Essential Oil of Algerian Ammodaucus leucotrichus\",\"authors\":\"Nesrine Sadaoui-Smadhi, S. Khemili-Talbi, Wadood Abdul, S. Toubal, W. Mokhtari, N. Benhabyles, K. Arab, Khettal Bachra, R. Fazal\",\"doi\":\"10.3844/ajbsp.2019.42.45\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"In a continuation of our previous work for the exploration of novel enzyme inhibitors, molecular modeling was used to inspect the binding mode of perillaldehyde and D-limonene, the major compounds of essential oil of Algerian Ammodaucus leucotrichus into the active site pocket of cholinesterase (AChE and BuChE) and Monoamine Oxidase (MAO). The molecular docking was carried out using Molecular Operating Environment (MOE) software package. Docking analysis showed that this compounds (perilladehyde and D-limonene) can interact with both the Catalytic Active Site (CAS) of AChE, BuChE and MAO. For D-limonene, molecular docking showed favorable H-phi interaction with catalytic residue of AchE and BuChE. The perillaldehyde showed best interaction profile with BuChE as compared with compound D-Limonene. The best interaction between perilladehyde and monoamine oxidase was also revealed. This paper shows best correlation between the in vitro study and the in silico molecular docking study of anti-cholinesterase and anti-monoamine oxidase activities.\",\"PeriodicalId\":11025,\"journal\":{\"name\":\"Current Research in Bioinformatics\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2019-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Current Research in Bioinformatics\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.3844/ajbsp.2019.42.45\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current Research in Bioinformatics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3844/ajbsp.2019.42.45","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
In Silico Cholinesterase and Monoamine Oxidase Inhibitory Activities of Perillaldehyde and D-Limonene, Main Compounds of Essential Oil of Algerian Ammodaucus leucotrichus
In a continuation of our previous work for the exploration of novel enzyme inhibitors, molecular modeling was used to inspect the binding mode of perillaldehyde and D-limonene, the major compounds of essential oil of Algerian Ammodaucus leucotrichus into the active site pocket of cholinesterase (AChE and BuChE) and Monoamine Oxidase (MAO). The molecular docking was carried out using Molecular Operating Environment (MOE) software package. Docking analysis showed that this compounds (perilladehyde and D-limonene) can interact with both the Catalytic Active Site (CAS) of AChE, BuChE and MAO. For D-limonene, molecular docking showed favorable H-phi interaction with catalytic residue of AchE and BuChE. The perillaldehyde showed best interaction profile with BuChE as compared with compound D-Limonene. The best interaction between perilladehyde and monoamine oxidase was also revealed. This paper shows best correlation between the in vitro study and the in silico molecular docking study of anti-cholinesterase and anti-monoamine oxidase activities.