A Study of the Active Site of Influenza Virus Sialidase: An Approach to the Rational Design of Novel Anti-influenza Drugs
The development of sialidase inhibitor-based potential anti-influenza drugs using rational drug design techniques has been of recent interest. The present study details an investigation of the active site of influenza virus sialidase by using the program GRID in an attempt to design more potent inhi...
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| Veröffentlicht in: | Journal of medicinal chemistry 1996-01, Vol.39 (2), p.388-391 |
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| container_end_page | 391 |
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| container_issue | 2 |
| container_start_page | 388 |
| container_title | Journal of medicinal chemistry |
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| creator | von Itzstein, Mark Dyason, Jeffrey C Oliver, Stuart W White, Hume F Wu, Wen-Yang Kok, Gaik B Pegg, Michael S |
| description | The development of sialidase inhibitor-based potential anti-influenza drugs using rational drug design techniques has been of recent interest. The present study details an investigation of the active site of influenza virus sialidase by using the program GRID in an attempt to design more potent inhibitors in the hope they will eventually lead to anti-influenza drugs. A number of different probes (amino, carboxy, hydroxy, methyl, etc.) have been used in an effort to determine the functional groups most likely to improve the binding of the starting template 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en). The data have correctly predicted the binding regions for the carboxylate, acetamido (NH and methyl), and glycerol (OH) groups of N-acetylneuraminic acid. Moreover, the data suggest that the addition of certain functionalities (amino group) at the C-4 position should enhance the overall binding. |
| doi_str_mv | 10.1021/jm950294c |
| format | Article |
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The present study details an investigation of the active site of influenza virus sialidase by using the program GRID in an attempt to design more potent inhibitors in the hope they will eventually lead to anti-influenza drugs. A number of different probes (amino, carboxy, hydroxy, methyl, etc.) have been used in an effort to determine the functional groups most likely to improve the binding of the starting template 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en). The data have correctly predicted the binding regions for the carboxylate, acetamido (NH and methyl), and glycerol (OH) groups of N-acetylneuraminic acid. Moreover, the data suggest that the addition of certain functionalities (amino group) at the C-4 position should enhance the overall binding.</description><identifier>ISSN: 0022-2623</identifier><identifier>EISSN: 1520-4804</identifier><identifier>DOI: 10.1021/jm950294c</identifier><identifier>PMID: 8558506</identifier><identifier>CODEN: JMCMAR</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents ; Antiviral agents ; Antiviral Agents - chemical synthesis ; Antiviral Agents - pharmacology ; Binding Sites ; Biological and medical sciences ; Computer Simulation ; Drug Design ; Medical sciences ; Molecular Probes ; Neuraminidase - chemistry ; Neuraminidase - metabolism ; Orthomyxoviridae - drug effects ; Orthomyxoviridae - enzymology ; Pharmacology. Drug treatments ; Protein Conformation</subject><ispartof>Journal of medicinal chemistry, 1996-01, Vol.39 (2), p.388-391</ispartof><rights>Copyright © 1996 American Chemical Society</rights><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a443t-55f2d1cc61b435b17c730a946a16036cb4e572cd2bd58901b5fdb4cbb7e152ac3</citedby><cites>FETCH-LOGICAL-a443t-55f2d1cc61b435b17c730a946a16036cb4e572cd2bd58901b5fdb4cbb7e152ac3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jm950294c$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jm950294c$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2965383$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8558506$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>von Itzstein, Mark</creatorcontrib><creatorcontrib>Dyason, Jeffrey C</creatorcontrib><creatorcontrib>Oliver, Stuart W</creatorcontrib><creatorcontrib>White, Hume F</creatorcontrib><creatorcontrib>Wu, Wen-Yang</creatorcontrib><creatorcontrib>Kok, Gaik B</creatorcontrib><creatorcontrib>Pegg, Michael S</creatorcontrib><title>A Study of the Active Site of Influenza Virus Sialidase: An Approach to the Rational Design of Novel Anti-influenza Drugs</title><title>Journal of medicinal chemistry</title><addtitle>J. Med. Chem</addtitle><description>The development of sialidase inhibitor-based potential anti-influenza drugs using rational drug design techniques has been of recent interest. The present study details an investigation of the active site of influenza virus sialidase by using the program GRID in an attempt to design more potent inhibitors in the hope they will eventually lead to anti-influenza drugs. A number of different probes (amino, carboxy, hydroxy, methyl, etc.) have been used in an effort to determine the functional groups most likely to improve the binding of the starting template 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en). The data have correctly predicted the binding regions for the carboxylate, acetamido (NH and methyl), and glycerol (OH) groups of N-acetylneuraminic acid. Moreover, the data suggest that the addition of certain functionalities (amino group) at the C-4 position should enhance the overall binding.</description><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>Antiviral agents</subject><subject>Antiviral Agents - chemical synthesis</subject><subject>Antiviral Agents - pharmacology</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Computer Simulation</subject><subject>Drug Design</subject><subject>Medical sciences</subject><subject>Molecular Probes</subject><subject>Neuraminidase - chemistry</subject><subject>Neuraminidase - metabolism</subject><subject>Orthomyxoviridae - drug effects</subject><subject>Orthomyxoviridae - enzymology</subject><subject>Pharmacology. 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Antiinfectious agents. Antiparasitic agents</topic><topic>Antiviral agents</topic><topic>Antiviral Agents - chemical synthesis</topic><topic>Antiviral Agents - pharmacology</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Computer Simulation</topic><topic>Drug Design</topic><topic>Medical sciences</topic><topic>Molecular Probes</topic><topic>Neuraminidase - chemistry</topic><topic>Neuraminidase - metabolism</topic><topic>Orthomyxoviridae - drug effects</topic><topic>Orthomyxoviridae - enzymology</topic><topic>Pharmacology. Drug treatments</topic><topic>Protein Conformation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>von Itzstein, Mark</creatorcontrib><creatorcontrib>Dyason, Jeffrey C</creatorcontrib><creatorcontrib>Oliver, Stuart W</creatorcontrib><creatorcontrib>White, Hume F</creatorcontrib><creatorcontrib>Wu, Wen-Yang</creatorcontrib><creatorcontrib>Kok, Gaik B</creatorcontrib><creatorcontrib>Pegg, Michael S</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of medicinal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>von Itzstein, Mark</au><au>Dyason, Jeffrey C</au><au>Oliver, Stuart W</au><au>White, Hume F</au><au>Wu, Wen-Yang</au><au>Kok, Gaik B</au><au>Pegg, Michael S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Study of the Active Site of Influenza Virus Sialidase: An Approach to the Rational Design of Novel Anti-influenza Drugs</atitle><jtitle>Journal of medicinal chemistry</jtitle><addtitle>J. Med. Chem</addtitle><date>1996-01-19</date><risdate>1996</risdate><volume>39</volume><issue>2</issue><spage>388</spage><epage>391</epage><pages>388-391</pages><issn>0022-2623</issn><eissn>1520-4804</eissn><coden>JMCMAR</coden><abstract>The development of sialidase inhibitor-based potential anti-influenza drugs using rational drug design techniques has been of recent interest. The present study details an investigation of the active site of influenza virus sialidase by using the program GRID in an attempt to design more potent inhibitors in the hope they will eventually lead to anti-influenza drugs. A number of different probes (amino, carboxy, hydroxy, methyl, etc.) have been used in an effort to determine the functional groups most likely to improve the binding of the starting template 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en). The data have correctly predicted the binding regions for the carboxylate, acetamido (NH and methyl), and glycerol (OH) groups of N-acetylneuraminic acid. Moreover, the data suggest that the addition of certain functionalities (amino group) at the C-4 position should enhance the overall binding.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>8558506</pmid><doi>10.1021/jm950294c</doi><tpages>4</tpages></addata></record> |
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| ispartof | Journal of medicinal chemistry, 1996-01, Vol.39 (2), p.388-391 |
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| language | eng |
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| source | ACS Publications; MEDLINE |
| subjects | Antibiotics. Antiinfectious agents. Antiparasitic agents Antiviral agents Antiviral Agents - chemical synthesis Antiviral Agents - pharmacology Binding Sites Biological and medical sciences Computer Simulation Drug Design Medical sciences Molecular Probes Neuraminidase - chemistry Neuraminidase - metabolism Orthomyxoviridae - drug effects Orthomyxoviridae - enzymology Pharmacology. Drug treatments Protein Conformation |
| title | A Study of the Active Site of Influenza Virus Sialidase: An Approach to the Rational Design of Novel Anti-influenza Drugs |
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