Novel 3,4-disubstituted-Neu5Ac2en derivatives as probes to investigate flexibility of the influenza virus sialidase 150-loop.
Identifieur interne : 000119 ( PubMed/Curation ); précédent : 000118; suivant : 000120Novel 3,4-disubstituted-Neu5Ac2en derivatives as probes to investigate flexibility of the influenza virus sialidase 150-loop.
Auteurs : Santosh Rudrawar [Australie] ; Jeffrey C. Dyason ; Andrea Maggioni ; Robin J. Thomson ; Mark Von ItzsteinSource :
- Bioorganic & medicinal chemistry [ 1464-3391 ] ; 2013.
Descripteurs français
- KwdFr :
- MESH :
- analogues et dérivés : Acide N-acétyl-neuraminique.
- enzymologie : Orthomyxoviridae.
- métabolisme : Acide N-acétyl-neuraminique, Sialidase.
- Acide N-acétyl-neuraminique, Acides sialiques, Liaison aux protéines, Sialidase, Sondes moléculaires, Structure secondaire des protéines.
English descriptors
- KwdEn :
- Molecular Probes, N-Acetylneuraminic Acid (analogs & derivatives), N-Acetylneuraminic Acid (chemistry), N-Acetylneuraminic Acid (metabolism), Neuraminidase (chemistry), Neuraminidase (metabolism), Orthomyxoviridae (enzymology), Protein Binding, Protein Structure, Secondary, Sialic Acids (chemistry).
- MESH :
- chemical , analogs & derivatives : N-Acetylneuraminic Acid.
- chemical , chemistry : N-Acetylneuraminic Acid, Neuraminidase, Sialic Acids.
- chemical , metabolism : N-Acetylneuraminic Acid, Neuraminidase.
- chemical : Molecular Probes.
- enzymology : Orthomyxoviridae.
- Protein Binding, Protein Structure, Secondary.
Abstract
Novel 3,4-disubstituted-Neu5Ac2en derivatives have been synthesised to probe the open 150-loop conformation of influenza virus sialidases. Both equatorially and axially (epi) substituted C4 amino and guanidino 3-(p-tolyl)allyl-Neu5Ac2en derivatives were prepared, via the 4-epi-hydroxy derivative. The equatorially-substituted 4-amino derivative showed low micromolar inhibition of both group-1 (pdm09 H1N1) and group-2 (pdm57 H2N2) sialidases, and provides the first in vitro evidence that a group-2 sialidase may exhibit 150-loop flexibility.
DOI: 10.1016/j.bmc.2013.05.054
PubMed: 23800724
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Dyason</name></author><author><name sortKey="Maggioni, Andrea" sort="Maggioni, Andrea" uniqKey="Maggioni A" first="Andrea" last="Maggioni">Andrea Maggioni</name></author><author><name sortKey="Thomson, Robin J" sort="Thomson, Robin J" uniqKey="Thomson R" first="Robin J" last="Thomson">Robin J. Thomson</name></author><author><name sortKey="Von Itzstein, Mark" sort="Von Itzstein, Mark" uniqKey="Von Itzstein M" first="Mark" last="Von Itzstein">Mark Von Itzstein</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23800724</idno><idno type="pmid">23800724</idno><idno type="doi">10.1016/j.bmc.2013.05.054</idno><idno type="wicri:Area/PubMed/Corpus">000119</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000119</idno><idno type="wicri:Area/PubMed/Curation">000119</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000119</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Novel 3,4-disubstituted-Neu5Ac2en derivatives as probes to investigate flexibility of the influenza virus sialidase 150-loop.</title><author><name sortKey="Rudrawar, Santosh" sort="Rudrawar, Santosh" uniqKey="Rudrawar S" first="Santosh" last="Rudrawar">Santosh Rudrawar</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Glycomics, Griffith University, Gold Coast Campus, Queensland 4222, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Institute for Glycomics, Griffith University, Gold Coast Campus, Queensland 4222</wicri:regionArea></affiliation></author><author><name sortKey="Dyason, Jeffrey C" sort="Dyason, Jeffrey C" uniqKey="Dyason J" first="Jeffrey C" last="Dyason">Jeffrey C. 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Thomson</name></author><author><name sortKey="Von Itzstein, Mark" sort="Von Itzstein, Mark" uniqKey="Von Itzstein M" first="Mark" last="Von Itzstein">Mark Von Itzstein</name></author></analytic><series><title level="j">Bioorganic & medicinal chemistry</title><idno type="eISSN">1464-3391</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Molecular Probes</term><term>N-Acetylneuraminic Acid (analogs & derivatives)</term><term>N-Acetylneuraminic Acid (chemistry)</term><term>N-Acetylneuraminic Acid (metabolism)</term><term>Neuraminidase (chemistry)</term><term>Neuraminidase (metabolism)</term><term>Orthomyxoviridae (enzymology)</term><term>Protein Binding</term><term>Protein Structure, Secondary</term><term>Sialic Acids (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide N-acétyl-neuraminique ()</term><term>Acide N-acétyl-neuraminique (analogues et dérivés)</term><term>Acide N-acétyl-neuraminique (métabolisme)</term><term>Acides sialiques ()</term><term>Liaison aux protéines</term><term>Orthomyxoviridae (enzymologie)</term><term>Sialidase ()</term><term>Sialidase (métabolisme)</term><term>Sondes moléculaires</term><term>Structure secondaire des protéines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>N-Acetylneuraminic Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>N-Acetylneuraminic Acid</term><term>Neuraminidase</term><term>Sialic Acids</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>N-Acetylneuraminic Acid</term><term>Neuraminidase</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Molecular Probes</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Acide N-acétyl-neuraminique</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Orthomyxoviridae</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Orthomyxoviridae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide N-acétyl-neuraminique</term><term>Sialidase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Protein Binding</term><term>Protein Structure, Secondary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Acide N-acétyl-neuraminique</term><term>Acides sialiques</term><term>Liaison aux protéines</term><term>Sialidase</term><term>Sondes moléculaires</term><term>Structure secondaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Novel 3,4-disubstituted-Neu5Ac2en derivatives have been synthesised to probe the open 150-loop conformation of influenza virus sialidases. Both equatorially and axially (epi) substituted C4 amino and guanidino 3-(p-tolyl)allyl-Neu5Ac2en derivatives were prepared, via the 4-epi-hydroxy derivative. The equatorially-substituted 4-amino derivative showed low micromolar inhibition of both group-1 (pdm09 H1N1) and group-2 (pdm57 H2N2) sialidases, and provides the first in vitro evidence that a group-2 sialidase may exhibit 150-loop flexibility. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23800724</PMID><DateCompleted><Year>2014</Year><Month>02</Month><Day>19</Day></DateCompleted><DateRevised><Year>2013</Year><Month>07</Month><Day>23</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1464-3391</ISSN><JournalIssue CitedMedium="Internet"><Volume>21</Volume><Issue>16</Issue><PubDate><Year>2013</Year><Month>Aug</Month><Day>15</Day></PubDate></JournalIssue><Title>Bioorganic & medicinal chemistry</Title><ISOAbbreviation>Bioorg. Med. Chem.</ISOAbbreviation></Journal><ArticleTitle>Novel 3,4-disubstituted-Neu5Ac2en derivatives as probes to investigate flexibility of the influenza virus sialidase 150-loop.</ArticleTitle><Pagination><MedlinePgn>4820-30</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bmc.2013.05.054</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0968-0896(13)00503-8</ELocationID><Abstract><AbstractText>Novel 3,4-disubstituted-Neu5Ac2en derivatives have been synthesised to probe the open 150-loop conformation of influenza virus sialidases. Both equatorially and axially (epi) substituted C4 amino and guanidino 3-(p-tolyl)allyl-Neu5Ac2en derivatives were prepared, via the 4-epi-hydroxy derivative. The equatorially-substituted 4-amino derivative showed low micromolar inhibition of both group-1 (pdm09 H1N1) and group-2 (pdm57 H2N2) sialidases, and provides the first in vitro evidence that a group-2 sialidase may exhibit 150-loop flexibility. </AbstractText><CopyrightInformation>Copyright © 2013 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rudrawar</LastName><ForeName>Santosh</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Institute for Glycomics, Griffith University, Gold Coast Campus, Queensland 4222, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dyason</LastName><ForeName>Jeffrey C</ForeName><Initials>JC</Initials></Author><Author ValidYN="Y"><LastName>Maggioni</LastName><ForeName>Andrea</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Thomson</LastName><ForeName>Robin J</ForeName><Initials>RJ</Initials></Author><Author ValidYN="Y"><LastName>von Itzstein</LastName><ForeName>Mark</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>06</Month><Day>06</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Bioorg Med Chem</MedlineTA><NlmUniqueID>9413298</NlmUniqueID><ISSNLinking>0968-0896</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015335">Molecular Probes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012794">Sialic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>24967-27-9</RegistryNumber><NameOfSubstance UI="C036137">2-deoxy-2,3-dehydro-N-acetylneuraminic acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.18</RegistryNumber><NameOfSubstance UI="D009439">Neuraminidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GZP2782OP0</RegistryNumber><NameOfSubstance UI="D019158">N-Acetylneuraminic Acid</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D015335" MajorTopicYN="N">Molecular Probes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019158" MajorTopicYN="N">N-Acetylneuraminic Acid</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009439" MajorTopicYN="N">Neuraminidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009975" MajorTopicYN="N">Orthomyxoviridae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012794" MajorTopicYN="N">Sialic Acids</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">150-loop</Keyword><Keyword MajorTopicYN="N">Influenza</Keyword><Keyword MajorTopicYN="N">Neu5Ac2en</Keyword><Keyword MajorTopicYN="N">Sialic acid</Keyword><Keyword MajorTopicYN="N">Sialidase</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>12</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>04</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>05</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>6</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>6</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>2</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23800724</ArticleId><ArticleId IdType="pii">S0968-0896(13)00503-8</ArticleId><ArticleId IdType="doi">10.1016/j.bmc.2013.05.054</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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