Correlation of the dynamics of native human acetylcholinesterase and its inhibited huperzine A counterpart from sub-picoseconds to nanoseconds.
Identifieur interne : 003713 ( PubMed/Checkpoint ); précédent : 003712; suivant : 003714Correlation of the dynamics of native human acetylcholinesterase and its inhibited huperzine A counterpart from sub-picoseconds to nanoseconds.
Auteurs : M. Trapp [Allemagne] ; M. Tehei [Australie] ; M. Trovaslet [France] ; F. Nachon [France] ; N. Martinez [France] ; M M Koza [France] ; M. Weik [France] ; P. Masson [France] ; J. Peters [France]Source :
- Journal of the Royal Society, Interface [ 1742-5662 ] ; 2014.
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Abstract
It is a long debated question whether catalytic activities of enzymes, which lie on the millisecond timescale, are possibly already reflected in variations in atomic thermal fluctuations on the pico- to nanosecond timescale. To shed light on this puzzle, the enzyme human acetylcholinesterase in its wild-type form and complexed with the inhibitor huperzine A were investigated by various neutron scattering techniques and molecular dynamics simulations. Previous results on elastic neutron scattering at various timescales and simulations suggest that dynamical processes are not affected on average by the presence of the ligand within the considered time ranges between 10 ps and 1 ns. In the work presented here, the focus was laid on quasi-elastic (QENS) and inelastic neutron scattering (INS). These techniques give access to different kinds of individual diffusive motions and to the density of states of collective motions at the sub-picoseconds timescale. Hence, they permit going beyond the first approach of looking at mean square displacements. For both samples, the autocorrelation function was well described by a stretched-exponential function indicating a linkage between the timescales of fast and slow functional relaxation dynamics. The findings of the QENS and INS investigation are discussed in relation to the results of our earlier elastic incoherent neutron scattering and molecular dynamics simulations.
DOI: 10.1098/rsif.2014.0372
PubMed: 24872501
Affiliations:
- Allemagne, Australie, France
- Auvergne-Rhône-Alpes, Berlin, Rhône-Alpes
- Berlin, Grenoble
- Université Joseph Fourier
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Ebel, UMR 5075, CNRS-CEA-UJF, 38042 Grenoble Cédex 9, France Institut de Recherche Biomédicale des Armées, 91223 Brétigny sur Orge</wicri:regionArea><wicri:noRegion>91223 Brétigny sur Orge</wicri:noRegion><wicri:noRegion>91223 Brétigny sur Orge</wicri:noRegion></affiliation></author><author><name sortKey="Martinez, N" sort="Martinez, N" uniqKey="Martinez N" first="N" last="Martinez">N. Martinez</name><affiliation wicri:level="4"><nlm:affiliation>Institut de Biologie Structurale J.-P. Ebel, UMR 5075, CNRS-CEA-UJF, 38042 Grenoble Cédex 9, France Institut Laue Langevin, 38042 Grenoble Cédex 9, France Université Joseph Fourier, UFR PhITEM, 38041 Grenoble Cédex 9, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut de Biologie Structurale J.-P. 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Ebel, UMR 5075, CNRS-CEA-UJF, 38042 Grenoble Cédex 9</wicri:regionArea><wicri:noRegion>38042 Grenoble Cédex 9</wicri:noRegion><wicri:noRegion>38042 Grenoble Cédex 9</wicri:noRegion></affiliation></author><author><name sortKey="Peters, J" sort="Peters, J" uniqKey="Peters J" first="J" last="Peters">J. Peters</name><affiliation wicri:level="4"><nlm:affiliation>Institut de Biologie Structurale J.-P. Ebel, UMR 5075, CNRS-CEA-UJF, 38042 Grenoble Cédex 9, France Institut Laue Langevin, 38042 Grenoble Cédex 9, France Université Joseph Fourier, UFR PhITEM, 38041 Grenoble Cédex 9, France jpeters@ill.eu.</nlm:affiliation><orgName type="university">Université Joseph Fourier</orgName><country>France</country><placeName><settlement type="city">Grenoble</settlement><region type="region" nuts="2">Auvergne-Rhône-Alpes</region><region type="old region" nuts="2">Rhône-Alpes</region></placeName></affiliation></author></analytic><series><title level="j">Journal of the Royal Society, Interface</title><idno type="eISSN">1742-5662</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acetylcholinesterase (chemistry)</term><term>Alkaloids (chemistry)</term><term>Binding Sites</term><term>Catalysis</term><term>Cholinesterase Inhibitors (chemistry)</term><term>Enzyme Activation</term><term>Humans</term><term>Kinetics</term><term>Models, Chemical</term><term>Molecular Dynamics Simulation</term><term>Protein Binding</term><term>Sesquiterpenes (chemistry)</term><term>Statistics as Topic</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acetylcholinesterase ()</term><term>Activation enzymatique</term><term>Alcaloïdes ()</term><term>Anticholinestérasiques ()</term><term>Catalyse</term><term>Cinétique</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles chimiques</term><term>Sesquiterpènes ()</term><term>Simulation de dynamique moléculaire</term><term>Sites de fixation</term><term>Statistiques comme sujet</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Acetylcholinesterase</term><term>Alkaloids</term><term>Cholinesterase Inhibitors</term><term>Sesquiterpenes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Catalysis</term><term>Enzyme Activation</term><term>Humans</term><term>Kinetics</term><term>Models, Chemical</term><term>Molecular Dynamics Simulation</term><term>Protein Binding</term><term>Statistics as Topic</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Acetylcholinesterase</term><term>Activation enzymatique</term><term>Alcaloïdes</term><term>Anticholinestérasiques</term><term>Catalyse</term><term>Cinétique</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles chimiques</term><term>Sesquiterpènes</term><term>Simulation de dynamique moléculaire</term><term>Sites de fixation</term><term>Statistiques comme sujet</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">It is a long debated question whether catalytic activities of enzymes, which lie on the millisecond timescale, are possibly already reflected in variations in atomic thermal fluctuations on the pico- to nanosecond timescale. To shed light on this puzzle, the enzyme human acetylcholinesterase in its wild-type form and complexed with the inhibitor huperzine A were investigated by various neutron scattering techniques and molecular dynamics simulations. Previous results on elastic neutron scattering at various timescales and simulations suggest that dynamical processes are not affected on average by the presence of the ligand within the considered time ranges between 10 ps and 1 ns. In the work presented here, the focus was laid on quasi-elastic (QENS) and inelastic neutron scattering (INS). These techniques give access to different kinds of individual diffusive motions and to the density of states of collective motions at the sub-picoseconds timescale. Hence, they permit going beyond the first approach of looking at mean square displacements. For both samples, the autocorrelation function was well described by a stretched-exponential function indicating a linkage between the timescales of fast and slow functional relaxation dynamics. The findings of the QENS and INS investigation are discussed in relation to the results of our earlier elastic incoherent neutron scattering and molecular dynamics simulations.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24872501</PMID><DateCreated><Year>2014</Year><Month>05</Month><Day>29</Day></DateCreated><DateCompleted><Year>2015</Year><Month>01</Month><Day>05</Day></DateCompleted><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1742-5662</ISSN><JournalIssue CitedMedium="Internet"><Volume>11</Volume><Issue>97</Issue><PubDate><Year>2014</Year><Month>Aug</Month><Day>06</Day></PubDate></JournalIssue><Title>Journal of the Royal Society, Interface</Title><ISOAbbreviation>J R Soc Interface</ISOAbbreviation></Journal><ArticleTitle>Correlation of the dynamics of native human acetylcholinesterase and its inhibited huperzine A counterpart from sub-picoseconds to nanoseconds.</ArticleTitle><Pagination><MedlinePgn>20140372</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1098/rsif.2014.0372</ELocationID><ELocationID EIdType="pii" ValidYN="Y">20140372</ELocationID><Abstract><AbstractText>It is a long debated question whether catalytic activities of enzymes, which lie on the millisecond timescale, are possibly already reflected in variations in atomic thermal fluctuations on the pico- to nanosecond timescale. To shed light on this puzzle, the enzyme human acetylcholinesterase in its wild-type form and complexed with the inhibitor huperzine A were investigated by various neutron scattering techniques and molecular dynamics simulations. Previous results on elastic neutron scattering at various timescales and simulations suggest that dynamical processes are not affected on average by the presence of the ligand within the considered time ranges between 10 ps and 1 ns. In the work presented here, the focus was laid on quasi-elastic (QENS) and inelastic neutron scattering (INS). These techniques give access to different kinds of individual diffusive motions and to the density of states of collective motions at the sub-picoseconds timescale. Hence, they permit going beyond the first approach of looking at mean square displacements. For both samples, the autocorrelation function was well described by a stretched-exponential function indicating a linkage between the timescales of fast and slow functional relaxation dynamics. The findings of the QENS and INS investigation are discussed in relation to the results of our earlier elastic incoherent neutron scattering and molecular dynamics simulations.</AbstractText><CopyrightInformation>© 2014 The Author(s) Published by the Royal Society. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Trapp</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Helmholtz-Zentrum Berlin für Materialien und Energie, Lise-Meitner Campus, Hahn-Meitner-Platz 1, 14109 Berlin, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tehei</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>School of Chemistry, University of Wollongong, New South Wales 2522, Australia Centre for Medical Bioscience, Australian Institute of Nuclear Science and Engineering (AINSE), Menai, New South Wales, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Trovaslet</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institut de Biologie Structurale J.-P. Ebel, UMR 5075, CNRS-CEA-UJF, 38042 Grenoble Cédex 9, France Institut de Recherche Biomédicale des Armées, 91223 Brétigny sur Orge, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nachon</LastName><ForeName>F</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Institut de Biologie Structurale J.-P. Ebel, UMR 5075, CNRS-CEA-UJF, 38042 Grenoble Cédex 9, France Institut de Recherche Biomédicale des Armées, 91223 Brétigny sur Orge, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Martinez</LastName><ForeName>N</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Institut de Biologie Structurale J.-P. Ebel, UMR 5075, CNRS-CEA-UJF, 38042 Grenoble Cédex 9, France Institut Laue Langevin, 38042 Grenoble Cédex 9, France Université Joseph Fourier, UFR PhITEM, 38041 Grenoble Cédex 9, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Koza</LastName><ForeName>M M</ForeName><Initials>MM</Initials><AffiliationInfo><Affiliation>Institut Laue Langevin, 38042 Grenoble Cédex 9, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Weik</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institut de Biologie Structurale J.-P. Ebel, UMR 5075, CNRS-CEA-UJF, 38042 Grenoble Cédex 9, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Masson</LastName><ForeName>P</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Institut de Biologie Structurale J.-P. Ebel, UMR 5075, CNRS-CEA-UJF, 38042 Grenoble Cédex 9, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Peters</LastName><ForeName>J</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Institut de Biologie Structurale J.-P. Ebel, UMR 5075, CNRS-CEA-UJF, 38042 Grenoble Cédex 9, France Institut Laue Langevin, 38042 Grenoble Cédex 9, France Université Joseph Fourier, UFR PhITEM, 38041 Grenoble Cédex 9, France jpeters@ill.eu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J R Soc Interface</MedlineTA><NlmUniqueID>101217269</NlmUniqueID><ISSNLinking>1742-5662</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000470">Alkaloids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002800">Cholinesterase Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012717">Sesquiterpenes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0111871I23</RegistryNumber><NameOfSubstance UI="C050426">huperzine A</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.1.7</RegistryNumber><NameOfSubstance UI="D000110">Acetylcholinesterase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>ChemMedChem. 2012 Mar 5;7(3):400-5</RefSource><PMID Version="1">22052791</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Phys Rev E Stat Nonlin Soft Matter Phys. 2009 Oct;80(4 Pt 1):041805</RefSource><PMID Version="1">19905331</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 1998 Aug 4;95(16):9280-3</RefSource><PMID Version="1">9689071</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Protein Sci. 2008 Apr;17(4):601-5</RefSource><PMID 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UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002800" MajorTopicYN="N">Cholinesterase Inhibitors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008956" MajorTopicYN="Y">Models, Chemical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D056004" MajorTopicYN="Y">Molecular Dynamics Simulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012717" MajorTopicYN="N">Sesquiterpenes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013223" MajorTopicYN="N">Statistics as Topic</DescriptorName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC4208370</OtherID><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">human acetylcholinesterase</Keyword><Keyword MajorTopicYN="N">molecular dynamics</Keyword><Keyword MajorTopicYN="N">motional correlation</Keyword><Keyword MajorTopicYN="N">neutron scattering</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>5</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>5</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>1</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24872501</ArticleId><ArticleId IdType="pii">rsif.2014.0372</ArticleId><ArticleId IdType="doi">10.1098/rsif.2014.0372</ArticleId><ArticleId IdType="pmc">PMC4208370</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li><li>Australie</li><li>France</li></country><region><li>Auvergne-Rhône-Alpes</li><li>Berlin</li><li>Rhône-Alpes</li></region><settlement><li>Berlin</li><li>Grenoble</li></settlement><orgName><li>Université Joseph Fourier</li></orgName></list><tree><country name="Allemagne"><region name="Berlin"><name sortKey="Trapp, M" sort="Trapp, M" uniqKey="Trapp M" first="M" last="Trapp">M. Trapp</name></region></country><country name="Australie"><noRegion><name sortKey="Tehei, M" sort="Tehei, M" uniqKey="Tehei M" first="M" last="Tehei">M. Tehei</name></noRegion></country><country name="France"><noRegion><name sortKey="Trovaslet, M" sort="Trovaslet, M" uniqKey="Trovaslet M" first="M" last="Trovaslet">M. Trovaslet</name></noRegion><name sortKey="Koza, M M" sort="Koza, M M" uniqKey="Koza M" first="M M" last="Koza">M M Koza</name><name sortKey="Martinez, N" sort="Martinez, N" uniqKey="Martinez N" first="N" last="Martinez">N. Martinez</name><name sortKey="Masson, P" sort="Masson, P" uniqKey="Masson P" first="P" last="Masson">P. Masson</name><name sortKey="Nachon, F" sort="Nachon, F" uniqKey="Nachon F" first="F" last="Nachon">F. Nachon</name><name sortKey="Peters, J" sort="Peters, J" uniqKey="Peters J" first="J" last="Peters">J. Peters</name><name sortKey="Weik, M" sort="Weik, M" uniqKey="Weik M" first="M" last="Weik">M. 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