Unsaturated N -acetyl- D-glucosaminuronic acid glycosides as inhibitors of influenza virus sialidase
Identifieur interne : 001722 ( Istex/Corpus ); précédent : 001721; suivant : 001723Unsaturated N -acetyl- D-glucosaminuronic acid glycosides as inhibitors of influenza virus sialidase
Auteurs : Maretta C. Mann ; Tasneem Islam ; Jeffrey C. Dyason ; Pas Florio ; Carolyn J. Trower ; Robin J. Thomson ; Mark Von ItzsteinSource :
- Glycoconjugate Journal [ 0282-0080 ] ; 2006.
Abstract
Abstract: The threat of pandemic influenza is a significant concern of governments worldwide. There is a very limited and relatively expensive armament to tackle such a pandemic should it occur. This fact provides much impetus to the scientific community for the discovery of new and less expensive anti-influenza drugs. Our longstanding interest in the inhibition of influenza virus sialidase, coupled with the development of simple carbohydrates that mimic an unsaturated derivative of the enzyme's naturally-occurring ligand, N-acetylneuraminic acid, has led us to investigate the development of influenza virus sialidase inhibitors based on these mimetics. We have successfully prepared a range of these compounds, in good yield, from the relatively inexpensive carbohydrate N-acetylglucosamine utilising a short synthetic procedure. We have employed a sialidase inhibition assay for biological evaluation of the target compounds and to our delight these mimetics have displayed significant inhibition of influenza virus sialidase.
Url:
DOI: 10.1007/s10719-006-5445-9
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There is a very limited and relatively expensive armament to tackle such a pandemic should it occur. This fact provides much impetus to the scientific community for the discovery of new and less expensive anti-influenza drugs. Our longstanding interest in the inhibition of influenza virus sialidase, coupled with the development of simple carbohydrates that mimic an unsaturated derivative of the enzyme's naturally-occurring ligand, N-acetylneuraminic acid, has led us to investigate the development of influenza virus sialidase inhibitors based on these mimetics. We have successfully prepared a range of these compounds, in good yield, from the relatively inexpensive carbohydrate N-acetylglucosamine utilising a short synthetic procedure. We have employed a sialidase inhibition assay for biological evaluation of the target compounds and to our delight these mimetics have displayed significant inhibition of influenza virus sialidase.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>Maretta C. Mann</name><affiliations><json:string>Institute for Glycomics, Griffith University, Gold Coast Campus, PMB 50 Gold Coast Mail Centre, 9726, Queensland, Australia</json:string></affiliations></json:item><json:item><name>Tasneem Islam</name><affiliations><json:string>Institute for Glycomics, Griffith University, Gold Coast Campus, PMB 50 Gold Coast Mail Centre, 9726, Queensland, Australia</json:string></affiliations></json:item><json:item><name>Jeffrey C. 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There is a very limited and relatively expensive armament to tackle such a pandemic should it occur. This fact provides much impetus to the scientific community for the discovery of new and less expensive anti-influenza drugs. Our longstanding interest in the inhibition of influenza virus sialidase, coupled with the development of simple carbohydrates that mimic an unsaturated derivative of the enzyme's naturally-occurring ligand, N-acetylneuraminic acid, has led us to investigate the development of influenza virus sialidase inhibitors based on these mimetics. We have successfully prepared a range of these compounds, in good yield, from the relatively inexpensive carbohydrate N-acetylglucosamine utilising a short synthetic procedure. 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DisplayOrder="Western"><GivenName>Tasneem</GivenName><FamilyName>Islam</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Jeffrey</GivenName><GivenName>C.</GivenName><FamilyName>Dyason</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>Pas</GivenName><FamilyName>Florio</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1 Aff2"><AuthorName DisplayOrder="Western"><GivenName>Carolyn</GivenName><GivenName>J.</GivenName><FamilyName>Trower</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Robin</GivenName><GivenName>J.</GivenName><FamilyName>Thomson</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1" CorrespondingAffiliationID="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Mark</GivenName><GivenName>von</GivenName><FamilyName>Itzstein</FamilyName></AuthorName><Contact><Phone>+61-7-55527025</Phone><Fax>+61-7-55529040</Fax><Email>m.vonitzstein@griffith.edu.au</Email></Contact></Author><Affiliation ID="Aff1"><OrgDivision>Institute for Glycomics</OrgDivision><OrgName>Griffith University</OrgName><OrgAddress><Street>Gold Coast Campus, PMB 50 Gold Coast Mail Centre</Street><City>Queensland</City><Postcode>9726</Postcode><Country Code="AU">Australia</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgDivision>Department of Medicinal Chemistry</OrgDivision><OrgName>Monash University</OrgName><OrgAddress><Street>Parkville Campus</Street><City>Victoria</City><Country Code="AU">Australia</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading><Para>The threat of pandemic influenza is a significant concern of governments worldwide. There is a very limited and relatively expensive armament to tackle such a pandemic should it occur. This fact provides much impetus to the scientific community for the discovery of new and less expensive anti-influenza drugs. Our longstanding interest in the inhibition of influenza virus sialidase, coupled with the development of simple carbohydrates that mimic an unsaturated derivative of the enzyme's naturally-occurring ligand, <Emphasis Type="Italic">N</Emphasis>-acetylneuraminic acid, has led us to investigate the development of influenza virus sialidase inhibitors based on these mimetics. We have successfully prepared a range of these compounds, in good yield, from the relatively inexpensive carbohydrate <Emphasis Type="Italic">N</Emphasis>-acetylglucosamine utilising a short synthetic procedure. We have employed a sialidase inhibition assay for biological evaluation of the target compounds and to our delight these mimetics have displayed significant inhibition of influenza virus sialidase.</Para></Abstract><KeywordGroup Language="En"><Heading>Keywords</Heading><Keyword>Influenza virus</Keyword><Keyword>Sialidase</Keyword><Keyword>Sialylmimetics</Keyword><Keyword>Sialic acids</Keyword><Keyword>Inhibitors</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Unsaturated N -acetyl- D-glucosaminuronic acid glycosides as inhibitors of influenza virus sialidase</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Unsaturated N -acetyl- D-glucosaminuronic acid glycosides as inhibitors of influenza virus sialidase</title></titleInfo><name type="personal"><namePart type="given">Maretta</namePart><namePart type="given">C.</namePart><namePart type="family">Mann</namePart><affiliation>Institute for Glycomics, Griffith University, Gold Coast Campus, PMB 50 Gold Coast Mail Centre, 9726, Queensland, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Tasneem</namePart><namePart type="family">Islam</namePart><affiliation>Institute for Glycomics, Griffith University, Gold Coast Campus, PMB 50 Gold Coast Mail Centre, 9726, Queensland, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jeffrey</namePart><namePart type="given">C.</namePart><namePart type="family">Dyason</namePart><affiliation>Institute for Glycomics, Griffith University, Gold Coast Campus, PMB 50 Gold Coast Mail Centre, 9726, Queensland, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Pas</namePart><namePart type="family">Florio</namePart><affiliation>Department of Medicinal Chemistry, Monash University, Parkville Campus, Victoria, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Carolyn</namePart><namePart type="given">J.</namePart><namePart type="family">Trower</namePart><affiliation>Institute for Glycomics, Griffith University, Gold Coast Campus, PMB 50 Gold Coast Mail Centre, 9726, Queensland, Australia</affiliation><affiliation>Department of Medicinal Chemistry, Monash University, Parkville Campus, Victoria, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Robin</namePart><namePart type="given">J.</namePart><namePart type="family">Thomson</namePart><affiliation>Institute for Glycomics, Griffith University, Gold Coast Campus, PMB 50 Gold Coast Mail Centre, 9726, Queensland, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal" displayLabel="corresp"><namePart type="given">Mark</namePart><namePart type="given">von</namePart><namePart type="family">Itzstein</namePart><affiliation>Institute for Glycomics, Griffith University, Gold Coast Campus, PMB 50 Gold Coast Mail Centre, 9726, Queensland, Australia</affiliation><affiliation>E-mail: m.vonitzstein@griffith.edu.au</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>Kluwer Academic Publishers</publisher><place><placeTerm type="text">Boston</placeTerm></place><dateIssued encoding="w3cdtf">2006-02-01</dateIssued><copyrightDate encoding="w3cdtf">2006</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: The threat of pandemic influenza is a significant concern of governments worldwide. There is a very limited and relatively expensive armament to tackle such a pandemic should it occur. This fact provides much impetus to the scientific community for the discovery of new and less expensive anti-influenza drugs. Our longstanding interest in the inhibition of influenza virus sialidase, coupled with the development of simple carbohydrates that mimic an unsaturated derivative of the enzyme's naturally-occurring ligand, N-acetylneuraminic acid, has led us to investigate the development of influenza virus sialidase inhibitors based on these mimetics. We have successfully prepared a range of these compounds, in good yield, from the relatively inexpensive carbohydrate N-acetylglucosamine utilising a short synthetic procedure. We have employed a sialidase inhibition assay for biological evaluation of the target compounds and to our delight these mimetics have displayed significant inhibition of influenza virus sialidase.</abstract><subject lang="en"><genre>Keywords</genre><topic>Influenza virus</topic><topic>Sialidase</topic><topic>Sialylmimetics</topic><topic>Sialic acids</topic><topic>Inhibitors</topic></subject><relatedItem type="host"><titleInfo><title>Glycoconjugate Journal</title><subTitle>Official Journal of the International Glycoconjugate Organization</subTitle></titleInfo><titleInfo type="abbreviated"><title>Glycoconj J</title></titleInfo><name type="personal"><namePart type="given">Roland</namePart><namePart type="family">Schauer</namePart><role><roleTerm type="text">editor</roleTerm></role></name><name type="personal"><namePart type="given">Reinhard</namePart><namePart type="family">Vlasak</namePart><role><roleTerm type="text">editor</roleTerm></role></name><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>Springer</publisher><dateIssued encoding="w3cdtf">2006-02-01</dateIssued><copyrightDate encoding="w3cdtf">2006</copyrightDate></originInfo><subject><genre>Life Sciences</genre><topic>Pathology</topic><topic>Biochemistry, general</topic></subject><identifier type="ISSN">0282-0080</identifier><identifier type="eISSN">1573-4986</identifier><identifier type="JournalID">10719</identifier><identifier type="JournalSPIN">GLYC</identifier><identifier type="IssueArticleCount">16</identifier><identifier type="VolumeIssueCount">9</identifier><part><date>2006</date><detail type="issue"><title>Special Issue: Viruses and Sialic Acids</title></detail><detail type="volume"><number>23</number><caption>vol.</caption></detail><detail type="issue"><number>1-2</number><caption>no.</caption></detail><extent unit="pages"><start>127</start><end>133</end></extent></part><recordInfo><recordOrigin>Springer Science + Business Media, LLC, 2006</recordOrigin></recordInfo></relatedItem><identifier type="istex">A39EF8F827F6A1556DE42F876A052C1277F69727</identifier><identifier type="ark">ark:/67375/VQC-6R3JN5HQ-6</identifier><identifier type="DOI">10.1007/s10719-006-5445-9</identifier><identifier type="ArticleID">5445</identifier><identifier type="ArticleID">NO00005445</identifier><accessCondition type="use and reproduction" contentType="copyright">Springer Science + Business Media, LLC, 2006</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Converted from (version 1.2.14) to MODS version 3.6.</recordOrigin><recordCreationDate encoding="w3cdtf">2020-05-30</recordCreationDate></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-6R3JN5HQ-6/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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