Recent progress and challenges in the discovery of new neuraminidase inhibitors.
Identifieur interne : 001577 ( Ncbi/Merge ); précédent : 001576; suivant : 001578Recent progress and challenges in the discovery of new neuraminidase inhibitors.
Auteurs : Supakarn Chamni [Thaïlande] ; Wanchai De-EknamkulSource :
- Expert opinion on therapeutic patents [ 1744-7674 ] ; 2013.
Descripteurs français
- KwdFr :
- Animaux, Antienzymes (), Antienzymes (pharmacologie), Antiviraux (), Antiviraux (pharmacologie), Conception assistée par ordinateur, Conception de médicament, Conformation des protéines, Cristallographie aux rayons X, Dosage biologique, Découverte de médicament (), Grippe humaine (traitement médicamenteux), Grippe humaine (virologie), Humains, Orthomyxoviridae (), Orthomyxoviridae (enzymologie), Relation structure-activité, Sialidase (), Sialidase (antagonistes et inhibiteurs), Sialidase (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Sialidase.
- enzymologie : Orthomyxoviridae.
- métabolisme : Sialidase.
- pharmacologie : Antienzymes, Antiviraux.
- traitement médicamenteux : Grippe humaine.
- virologie : Grippe humaine.
- Animaux, Antienzymes, Antiviraux, Conception assistée par ordinateur, Conception de médicament, Conformation des protéines, Cristallographie aux rayons X, Dosage biologique, Découverte de médicament, Humains, Orthomyxoviridae, Relation structure-activité, Sialidase.
English descriptors
- KwdEn :
- Animals, Antiviral Agents (chemistry), Antiviral Agents (pharmacology), Biological Assay, Computer-Aided Design, Crystallography, X-Ray, Drug Design, Drug Discovery (methods), Enzyme Inhibitors (chemistry), Enzyme Inhibitors (pharmacology), Humans, Influenza, Human (drug therapy), Influenza, Human (virology), Neuraminidase (antagonists & inhibitors), Neuraminidase (chemistry), Neuraminidase (metabolism), Orthomyxoviridae (drug effects), Orthomyxoviridae (enzymology), Protein Conformation, Structure-Activity Relationship.
- MESH :
- chemical , antagonists & inhibitors : Neuraminidase.
- chemical , chemistry : Antiviral Agents, Enzyme Inhibitors, Neuraminidase.
- chemical , metabolism : Neuraminidase.
- chemical , pharmacology : Antiviral Agents, Enzyme Inhibitors.
- drug effects : Orthomyxoviridae.
- drug therapy : Influenza, Human.
- enzymology : Orthomyxoviridae.
- methods : Drug Discovery.
- virology : Influenza, Human.
- Animals, Biological Assay, Computer-Aided Design, Crystallography, X-Ray, Drug Design, Humans, Protein Conformation, Structure-Activity Relationship.
Abstract
At present, the key public health concern is to define the way in which the next influenza pandemic should be controlled. While influenza vaccines are available, their effectiveness could be significantly reduced if new strains differ significantly from those of the vaccines. Therefore, antiviral drugs play an important role in the prevention and management of influenza. The influenza neuraminidase (NA), a surface-glycoprotein enzyme involved in releasing the virus from the host cell, has been considered as an essential therapeutic target for treatment and prophylaxis of influenza infection. It is a highly conserved feature of the active site across all influenza A and B viruses and is of particular interest because compounds NA inhibitors (NAIs) can be cross-reactive against multiple types and subtypes of influenza. Currently, there are two NAI drugs which are licensed worldwide: oseltamivir and zanamivir, and two more drugs which have received recent approval in Japan: peramivir and laninamivir. Sudden changes in NAI susceptibility have stressed the urgent need in searching for novel inhibitors.
DOI: 10.1517/13543776.2013.765861
PubMed: 23369206
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xml:lang="en"><term>Antiviral Agents</term><term>Enzyme Inhibitors</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Sialidase</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Orthomyxoviridae</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Influenza, Human</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="methods" xml:lang="en"><term>Drug Discovery</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Sialidase</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antienzymes</term><term>Antiviraux</term></keywords><keywords scheme="MESH" qualifier="traitement médicamenteux" xml:lang="fr"><term>Grippe humaine</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Grippe humaine</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Influenza, Human</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Biological Assay</term><term>Computer-Aided Design</term><term>Crystallography, X-Ray</term><term>Drug Design</term><term>Humans</term><term>Protein Conformation</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Antienzymes</term><term>Antiviraux</term><term>Conception assistée par ordinateur</term><term>Conception de médicament</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Dosage biologique</term><term>Découverte de médicament</term><term>Humains</term><term>Orthomyxoviridae</term><term>Relation structure-activité</term><term>Sialidase</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">At present, the key public health concern is to define the way in which the next influenza pandemic should be controlled. While influenza vaccines are available, their effectiveness could be significantly reduced if new strains differ significantly from those of the vaccines. Therefore, antiviral drugs play an important role in the prevention and management of influenza. The influenza neuraminidase (NA), a surface-glycoprotein enzyme involved in releasing the virus from the host cell, has been considered as an essential therapeutic target for treatment and prophylaxis of influenza infection. It is a highly conserved feature of the active site across all influenza A and B viruses and is of particular interest because compounds NA inhibitors (NAIs) can be cross-reactive against multiple types and subtypes of influenza. Currently, there are two NAI drugs which are licensed worldwide: oseltamivir and zanamivir, and two more drugs which have received recent approval in Japan: peramivir and laninamivir. Sudden changes in NAI susceptibility have stressed the urgent need in searching for novel inhibitors.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23369206</PMID><DateCompleted><Year>2013</Year><Month>09</Month><Day>03</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>06</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1744-7674</ISSN><JournalIssue CitedMedium="Internet"><Volume>23</Volume><Issue>4</Issue><PubDate><Year>2013</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Expert opinion on therapeutic patents</Title><ISOAbbreviation>Expert Opin Ther Pat</ISOAbbreviation></Journal><ArticleTitle>Recent progress and challenges in the discovery of new neuraminidase inhibitors.</ArticleTitle><Pagination><MedlinePgn>409-23</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1517/13543776.2013.765861</ELocationID><Abstract><AbstractText Label="INTRODUCTION" NlmCategory="BACKGROUND">At present, the key public health concern is to define the way in which the next influenza pandemic should be controlled. While influenza vaccines are available, their effectiveness could be significantly reduced if new strains differ significantly from those of the vaccines. Therefore, antiviral drugs play an important role in the prevention and management of influenza. The influenza neuraminidase (NA), a surface-glycoprotein enzyme involved in releasing the virus from the host cell, has been considered as an essential therapeutic target for treatment and prophylaxis of influenza infection. It is a highly conserved feature of the active site across all influenza A and B viruses and is of particular interest because compounds NA inhibitors (NAIs) can be cross-reactive against multiple types and subtypes of influenza. Currently, there are two NAI drugs which are licensed worldwide: oseltamivir and zanamivir, and two more drugs which have received recent approval in Japan: peramivir and laninamivir. Sudden changes in NAI susceptibility have stressed the urgent need in searching for novel inhibitors.</AbstractText><AbstractText Label="AREAS COVERED" NlmCategory="METHODS">In this review, a potential pitfall in NA-based assays and the progress in the chemical synthesis of all patented NAIs from February 2006 to July 2012 are discussed.</AbstractText><AbstractText Label="EXPERT OPINION" NlmCategory="CONCLUSIONS">Both NA enzyme inhibition and X-ray crystallography data have suggested that the strategy of designing NAIs binding to the highly conserved region of NA can lead to inhibitors that are effective against all influenza NA subtypes. A number of new synthetic entries having unique structural frameworks that were designed based on computational study of X-ray structures of NA. They strongly exhibited the activity of NA in the low nanomolar range such as phosphonate congeners of zanamivir and oseltarmivir. Screening strategies based on the chemical diversity of natural products have revealed that flavonoids are the most prominent scaffolds possessing NA inhibitory activity. However, these substituted phenyl-benzopyrane compounds have been reported to exert a considerable quenching effect, causing false-positive results in the commonly used method of enzyme-based NA inhibition assays, and thus, reliability of the flavonoid-based NAIs reported in the literature.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chamni</LastName><ForeName>Supakarn</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Chulalongkorn University, Faculty of Pharmaceutical Sciences, Department of Pharmacognosy and Pharmaceutical Botany, Bangkok 10330, Thailand.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>De-Eknamkul</LastName><ForeName>Wanchai</ForeName><Initials>W</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType 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MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007251" MajorTopicYN="N">Influenza, Human</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="N">drug therapy</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009439" MajorTopicYN="N">Neuraminidase</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009975" MajorTopicYN="N">Orthomyxoviridae</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>2</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>2</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>9</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23369206</ArticleId><ArticleId IdType="doi">10.1517/13543776.2013.765861</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Thaïlande</li></country></list><tree><noCountry><name sortKey="De Eknamkul, Wanchai" sort="De Eknamkul, Wanchai" uniqKey="De Eknamkul W" first="Wanchai" last="De-Eknamkul">Wanchai De-Eknamkul</name></noCountry><country name="Thaïlande"><noRegion><name sortKey="Chamni, Supakarn" sort="Chamni, Supakarn" uniqKey="Chamni S" first="Supakarn" last="Chamni">Supakarn Chamni</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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