1 Ocak 2009 Dergi makalesi Açık Erişim

Khan, Mahmud Tareq Hassan; Orhan, I.; Senol, F. S.; Kartal, M.; Sener, B.; Dvorska, M.; Smejkal, K.; Slapetova, T.

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  <identifier identifierType="URL">https://aperta.ulakbim.gov.tr/record/41327</identifier>
  <creators>
    <creator>
      <creatorName>Khan, Mahmud Tareq Hassan</creatorName>
      <givenName>Mahmud Tareq Hassan</givenName>
      <familyName>Khan</familyName>
      <affiliation>Univ Tromso, Inst Med Biol, Dept Pharmacol, N-9037 Tromso, Norway</affiliation>
    </creator>
    <creator>
      <creatorName>Orhan, I.</creatorName>
      <givenName>I.</givenName>
      <familyName>Orhan</familyName>
      <affiliation>Gazi Univ, Fac Pharm, Dept Pharmacognosy, TR-06330 Ankara, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Senol, F. S.</creatorName>
      <givenName>F. S.</givenName>
      <familyName>Senol</familyName>
      <affiliation>Gazi Univ, Fac Pharm, Dept Pharmacognosy, TR-06330 Ankara, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Kartal, M.</creatorName>
      <givenName>M.</givenName>
      <familyName>Kartal</familyName>
      <affiliation>Ankara Univ, Fac Pharm, Dept Pharmacognosy, TR-06100 Ankara, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Sener, B.</creatorName>
      <givenName>B.</givenName>
      <familyName>Sener</familyName>
      <affiliation>Gazi Univ, Fac Pharm, Dept Pharmacognosy, TR-06330 Ankara, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Dvorska, M.</creatorName>
      <givenName>M.</givenName>
      <familyName>Dvorska</familyName>
      <affiliation>Univ Vet &amp; Pharmaceut Sci, Fac Pharm, Dept Nat Drugs, Brno 61242, Czech Republic</affiliation>
    </creator>
    <creator>
      <creatorName>Smejkal, K.</creatorName>
      <givenName>K.</givenName>
      <familyName>Smejkal</familyName>
      <affiliation>Univ Vet &amp; Pharmaceut Sci, Fac Pharm, Dept Nat Drugs, Brno 61242, Czech Republic</affiliation>
    </creator>
    <creator>
      <creatorName>Slapetova, T.</creatorName>
      <givenName>T.</givenName>
      <familyName>Slapetova</familyName>
      <affiliation>Univ Vet &amp; Pharmaceut Sci, Fac Pharm, Dept Nat Drugs, Brno 61242, Czech Republic</affiliation>
    </creator>
  </creators>
  <titles>
    <title>Cholinesterase Inhibitory Activities Of Some Flavonoid Derivatives And Chosen Xanthone And Their Molecular Docking Studies</title>
  </titles>
  <publisher>Aperta</publisher>
  <publicationYear>2009</publicationYear>
  <dates>
    <date dateType="Issued">2009-01-01</date>
  </dates>
  <resourceType resourceTypeGeneral="Text">Journal article</resourceType>
  <alternateIdentifiers>
    <alternateIdentifier alternateIdentifierType="url">https://aperta.ulakbim.gov.tr/record/41327</alternateIdentifier>
  </alternateIdentifiers>
  <relatedIdentifiers>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsIdenticalTo">10.1016/j.cbi.2009.06.024</relatedIdentifier>
  </relatedIdentifiers>
  <rightsList>
    <rights rightsURI="http://www.opendefinition.org/licenses/cc-by">Creative Commons Attribution</rights>
    <rights rightsURI="info:eu-repo/semantics/openAccess">Open Access</rights>
  </rightsList>
  <descriptions>
    <description descriptionType="Abstract">Flavonoids are one of the largest classes of plant secondary metabolites and are known to possess a number of significant biological activities for human health. In this study, we examined in vitro acetylcholinesterase (ACH) and butyrylcholinesterase (BChE) inhibitory activities of four flavonoid derivatives - quercetin, rutin, kaempferol 3-O-beta-D-galactoside and macluraxanthone. The in vitro results showed that quercetin and macluraxanthone displayed a concentration-dependant inhibition of AChE and BChE. Macluraxanthone showed to be the most potent and specific inhibitor of both the enzymes having the IC(50) values of 8.47 and 29.8 mu M, respectively. The enzyme kinetic studies revealed that quercetin inhibited both the enzymes in competitive manner, whereas the mode of inhibition of macluraxanthone was noncompetitive against AChE and competitive against BChE. The inhibitory profiles of the compounds have been compared with standard AChE inhibitor galanthamine. To get insight of the intermolecular interactions, the molecular docking studies of these two compounds were performed at the active site 3D space of both the enzymes, using ICM-Dock (TM) module. Docking studies exhibited that macluraxanthone binds much more tightly with both the enzymes than quercetin. The calculated docking and binding energies also supported the in vitro inhibitory profiles (IC(50) values). Both the compounds showed several strong hydrogen bonds to several important amino acid residues of both the enzymes. A number of hydrophobic interactions could also explain the potency of the compounds to inhibit AChE and BChE. Crown Copyright (C) 2009 Published by Elsevier Ireland Ltd. All rights reserved.</description>
  </descriptions>
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