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  <Article>
    <Journal>
      <PublisherName>isfcppharmaspire</PublisherName>
      <JournalTitle>Pharmaspire</JournalTitle>
      <PISSN>C</PISSN>
      <EISSN>o</EISSN>
      <Volume-Issue/>
      <PartNumber/>
      <IssueTopic>Multidisciplinary</IssueTopic>
      <IssueLanguage>English</IssueLanguage>
      <Season/>
      <SpecialIssue>N</SpecialIssue>
      <SupplementaryIssue>N</SupplementaryIssue>
      <IssueOA>Y</IssueOA>
      <PubDate>
        <Year>-0001</Year>
        <Month>11</Month>
        <Day>30</Day>
      </PubDate>
      <ArticleType>Pharmaceutics</ArticleType>
      <ArticleTitle>Molecular docking analysis of substituted 2-(1-benzylpiperidin-4-yl)-5-phenoxy-1H-benzo[d]imidazole derivatives as Acetylcholinesterase inhibitors for the management of Alzheimer’s disease</ArticleTitle>
      <SubTitle/>
      <ArticleLanguage>English</ArticleLanguage>
      <ArticleOA>Y</ArticleOA>
      <FirstPage>0</FirstPage>
      <LastPage>0</LastPage>
      <AuthorList>
        <Author>
          <FirstName>Pooja</FirstName>
          <LastName>Chawla</LastName>
          <AuthorLanguage>English</AuthorLanguage>
          <Affiliation/>
          <CorrespondingAuthor>N</CorrespondingAuthor>
          <ORCID/>
        </Author>
      </AuthorList>
      <DOI/>
      <Abstract>The loss of cholinergic neurons in the brain and hippocampus is the hallmark of Alzheimer's disease. The hydrolyzing enzyme acetylcholinesterase has been identified as a potential treatment for Alzheimer's disease. One of the most significant scaffolds for AChE binding is benzyl piperidine, which is included in the medication donepezil. Along with benzimidazole, which early investigations have also shown to significantly inhibit AChE. This study includes in designing of hybrid of benzyl piperidine and benzimidazole as AChE inhibitors. The study revealed that B24, A24, and B8 showed the highest BBB permeability and binding affinities (-11.4 kcal/mol, 11.0 kcal/mol, and 11.1 kcal/mol, respectively). All the chemicals behaved similarly in the binding pocket of AChE. These important interactions between residues include those between Trp86, Tyr341, Ser293, and others. In order to stop the BBB from penetrating, polar substitutions on more than two locations were also identified. However, compound B24 is an exception. It will further proceeds for biological evaluation in future.</Abstract>
      <AbstractLanguage>English</AbstractLanguage>
      <Keywords>Alzheimer’s disease, acetylcholinesterase, benzyl piperidine, benzimidazole, molecular docking</Keywords>
      <URLs>
        <Abstract>https://isfcppharmaspire.com/ubijournal-v1copy/journals/abstract.php?article_id=14859&amp;title=Molecular docking analysis of substituted 2-(1-benzylpiperidin-4-yl)-5-phenoxy-1H-benzo[d]imidazole derivatives as Acetylcholinesterase inhibitors for the management of Alzheimer’s disease</Abstract>
      </URLs>
      <References>
        <ReferencesarticleTitle>References</ReferencesarticleTitle>
        <ReferencesfirstPage>16</ReferencesfirstPage>
        <ReferenceslastPage>19</ReferenceslastPage>
        <References/>
      </References>
    </Journal>
  </Article>
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