Recent Advances in Neuraminidase Inhibitor Development as Anti‐influenza Drugs
Identifieur interne : 000B09 ( Main/Exploration ); précédent : 000B08; suivant : 000B10Recent Advances in Neuraminidase Inhibitor Development as Anti‐influenza Drugs
Auteurs : Enguang Feng [République populaire de Chine] ; Deju Ye [République populaire de Chine] ; Jian Li [République populaire de Chine] ; Dengyou Zhang [République populaire de Chine] ; Jinfang Wang [République populaire de Chine] ; Fei Zhao [République populaire de Chine] ; Rolf Hilgenfeld [République populaire de Chine, Allemagne] ; Mingyue Zheng [République populaire de Chine] ; Hualiang Jiang [République populaire de Chine] ; Hong Liu [République populaire de Chine]Source :
- ChemMedChem [ 1860-7179 ] ; 2012-09.
English descriptors
- Teeft :
- Active pocket, Active site, Active sites, Agents chemother, Alkyl groups, Amino, Amino acid residues, Analogue, Antiviral, Antiviral activity, Antiviral agents, Arginine residues, Aromatic carboxylic acid, Avian, Avian influenza, Avian influenza virus, Benzene ring, Benzoic acid derivatives, Binding affinity, Binding mode, Bioorg, Carbocyclic analogues, Carboxylate, Cause resistance, Chand, Chem, Chemmedchem, Cheng, Chinese academy, Crystal structure, Crystal structures, Derivative, Drug design, Drug discovery, Ethyl groups, Expert opin, Glycerol side chain, Gmbh, Guanidino, Guanidino group, Host cells, Human influenza, Hydrophobic interaction, Hydroxy, Hydroxy group, Important role, Influenza, Influenza infection, Influenza virus, Influenza virus infection, Influenza virus infections, Influenza viruses, Inhibitor, Inhibitory, Inhibitory activities, Inhibitory activity, Itzstein, Kgaa, Laninamivir, Laver, Lett, Lipophilic side chain, Methyl group, Neuraminidase, Neuraminidase inhibitors, Oseltamivir, Oseltamivir carboxylate, Pandemic, Pentyloxy side chain, Peramivir, Phosphonate analogues, Rational drug design, Resistant virus strains, Sialic, Sialic acid, Target cells, Typical group, Vaccine, Verlag, Verlag gmbh, Virol, Virus, Virus entry, Wang, Weinheim, Weinheim chemmedchem, Yamashita, Zanamivir, Zhang.
Abstract
The recent emergence of the highly pathogenic H5N1 subtype of avian influenza virus (AIV) and of the new type of human influenza A (H1N1) have emphasized the need for the development of effective anti‐influenza drugs. Presently, neuraminidase (NA) inhibitors are widely used in the treatment and prophylaxis of human influenza virus infection, and tremendous efforts have been made to develop more potent NA inhibitors to combat resistance and new influenza viruses. In this review, we discuss the structural characteristics of NA catalytic domains and the recent developments of new NA inhibitors using structure‐based drug design strategies. These drugs include analogues of zanamivir, analogues of oseltamivir, analogues of peramivir, and analogues of aromatic carboxylic acid and present promising options for therapeutics or leads for further development of NA inhibitors that may be useful in the event of a future influenza pandemic.
Attacking back: The emergence of new and highly pathogenic influenza virus strains have emphasized the need for effective anti‐influenza drugs. Inhibition of neuraminidase (NA), which plays a key role in the life cycle of influenza, has become an attractive antiviral strategy, benefiting from structure‐based design approaches. Resistance to current NA inhibitors suggests that ongoing development of new molecules will afford better protection against possible future influenza outbreaks.
Url:
DOI: 10.1002/cmdc.201200155
Affiliations:
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acid</term><term>Avian</term><term>Avian influenza</term><term>Avian influenza virus</term><term>Benzene ring</term><term>Benzoic acid derivatives</term><term>Binding affinity</term><term>Binding mode</term><term>Bioorg</term><term>Carbocyclic analogues</term><term>Carboxylate</term><term>Cause resistance</term><term>Chand</term><term>Chem</term><term>Chemmedchem</term><term>Cheng</term><term>Chinese academy</term><term>Crystal structure</term><term>Crystal structures</term><term>Derivative</term><term>Drug design</term><term>Drug discovery</term><term>Ethyl groups</term><term>Expert opin</term><term>Glycerol side chain</term><term>Gmbh</term><term>Guanidino</term><term>Guanidino group</term><term>Host cells</term><term>Human influenza</term><term>Hydrophobic interaction</term><term>Hydroxy</term><term>Hydroxy group</term><term>Important role</term><term>Influenza</term><term>Influenza infection</term><term>Influenza virus</term><term>Influenza virus infection</term><term>Influenza 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chemmedchem</term><term>Yamashita</term><term>Zanamivir</term><term>Zhang</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The recent emergence of the highly pathogenic H5N1 subtype of avian influenza virus (AIV) and of the new type of human influenza A (H1N1) have emphasized the need for the development of effective anti‐influenza drugs. Presently, neuraminidase (NA) inhibitors are widely used in the treatment and prophylaxis of human influenza virus infection, and tremendous efforts have been made to develop more potent NA inhibitors to combat resistance and new influenza viruses. In this review, we discuss the structural characteristics of NA catalytic domains and the recent developments of new NA inhibitors using structure‐based drug design strategies. These drugs include analogues of zanamivir, analogues of oseltamivir, analogues of peramivir, and analogues of aromatic carboxylic acid and present promising options for therapeutics or leads for further development of NA inhibitors that may be useful in the event of a future influenza pandemic.</div><div type="abstract" xml:lang="en">Attacking back: The emergence of new and highly pathogenic influenza virus strains have emphasized the need for effective anti‐influenza drugs. Inhibition of neuraminidase (NA), which plays a key role in the life cycle of influenza, has become an attractive antiviral strategy, benefiting from structure‐based design approaches. Resistance to current NA inhibitors suggests that ongoing development of new molecules will afford better protection against possible future influenza outbreaks.</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>République populaire de Chine</li></country></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Feng, Enguang" sort="Feng, Enguang" uniqKey="Feng E" first="Enguang" last="Feng">Enguang Feng</name></noRegion><name sortKey="Hilgenfeld, Rolf" sort="Hilgenfeld, Rolf" uniqKey="Hilgenfeld R" first="Rolf" last="Hilgenfeld">Rolf Hilgenfeld</name><name sortKey="Jiang, Hualiang" sort="Jiang, Hualiang" uniqKey="Jiang H" first="Hualiang" last="Jiang">Hualiang Jiang</name><name sortKey="Li, Jian" sort="Li, Jian" uniqKey="Li J" first="Jian" last="Li">Jian Li</name><name sortKey="Liu, Hong" sort="Liu, Hong" uniqKey="Liu H" first="Hong" last="Liu">Hong Liu</name><name sortKey="Liu, Hong" sort="Liu, Hong" uniqKey="Liu H" first="Hong" last="Liu">Hong Liu</name><name sortKey="Liu, Hong" sort="Liu, Hong" uniqKey="Liu H" first="Hong" last="Liu">Hong Liu</name><name sortKey="Wang, Jinfang" sort="Wang, Jinfang" uniqKey="Wang J" first="Jinfang" last="Wang">Jinfang Wang</name><name sortKey="Ye, Deju" sort="Ye, Deju" uniqKey="Ye D" first="Deju" last="Ye">Deju Ye</name><name sortKey="Zhang, Dengyou" sort="Zhang, Dengyou" uniqKey="Zhang D" first="Dengyou" last="Zhang">Dengyou Zhang</name><name sortKey="Zhao, Fei" sort="Zhao, Fei" uniqKey="Zhao F" first="Fei" last="Zhao">Fei Zhao</name><name sortKey="Zheng, Mingyue" sort="Zheng, Mingyue" uniqKey="Zheng M" first="Mingyue" last="Zheng">Mingyue Zheng</name></country><country name="Allemagne"><noRegion><name sortKey="Hilgenfeld, Rolf" sort="Hilgenfeld, Rolf" uniqKey="Hilgenfeld R" first="Rolf" last="Hilgenfeld">Rolf Hilgenfeld</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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