Peptide Inhibitors of Hepatitis C Virus NS3 Protease
Hepatitis C virus (HCV) is a highly prevalent virus and one of the major agents of chronic hepatitis. Since HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. Peptide inhibitors of NS3 were developed by selective amino...
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| Veröffentlicht in: | Antiviral chemistry & chemotherapy 2003-10, Vol.14 (5), p.225-233 |
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| creator | Portal-Núñez, Sergio González-Navarro, Carlos J García-Delgado, Marina Vizmanos, José Luis Lasarte, Juan José Borrás-Cuesta, Francisco |
| description | Hepatitis C virus (HCV) is a highly prevalent virus and one of the major agents of chronic hepatitis. Since HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. Peptide inhibitors of NS3 were developed by selective amino acid replacement of six leader sequences, corresponding to regions of HCV polyprotein that are cleaved by NS3. The large numbers of potential 14-mer and 16-mer peptide inhibitors thus obtained were tested against NS3 using the fluorescent probe RETS1 and peptide cofactor SVVIVGRIILSGRA from NS4A protein. This afforded several peptide inhibitors with an IC50 of around 2 μM. These peptides may be good leading compounds for the development of peptidomimetics to control HCV replication in the treatment of chronic hepatitis C. |
| doi_str_mv | 10.1177/095632020301400501 |
| format | Article |
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Since HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. Peptide inhibitors of NS3 were developed by selective amino acid replacement of six leader sequences, corresponding to regions of HCV polyprotein that are cleaved by NS3. The large numbers of potential 14-mer and 16-mer peptide inhibitors thus obtained were tested against NS3 using the fluorescent probe RETS1 and peptide cofactor SVVIVGRIILSGRA from NS4A protein. This afforded several peptide inhibitors with an IC50 of around 2 μM. These peptides may be good leading compounds for the development of peptidomimetics to control HCV replication in the treatment of chronic hepatitis C.</description><identifier>ISSN: 2040-2066</identifier><identifier>ISSN: 0956-3202</identifier><identifier>EISSN: 2040-2066</identifier><identifier>DOI: 10.1177/095632020301400501</identifier><identifier>PMID: 14694985</identifier><language>eng</language><publisher>London, England: SAGE Publications</publisher><subject>Amino Acid Sequence ; Antibiotics. Antiinfectious agents. Antiparasitic agents ; Antiviral agents ; Antiviral Agents - chemistry ; Antiviral Agents - pharmacology ; Biological and medical sciences ; Fluorescent indicators ; Hepatitis ; Hepatitis C ; Hepatitis C - drug therapy ; Hepatitis C virus ; Humans ; Hydrolysis ; Inhibitory Concentration 50 ; Interferon ; Kinetics ; Medical sciences ; Molecular Mimicry ; NS4A protein ; Oligopeptides - chemistry ; Oligopeptides - pharmacology ; Peptide inhibitors ; Peptides ; Peptidomimetics ; Pharmacology. Drug treatments ; Protease Inhibitors - chemistry ; Protease Inhibitors - pharmacology ; Protein sorting signals ; Proteinase ; Replication ; Structure-Activity Relationship ; Viral Nonstructural Proteins - antagonists & inhibitors</subject><ispartof>Antiviral chemistry & chemotherapy, 2003-10, Vol.14 (5), p.225-233</ispartof><rights>2003 SAGE Publications</rights><rights>2004 INIST-CNRS</rights><rights>2003 SAGE Publications. 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Since HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. Peptide inhibitors of NS3 were developed by selective amino acid replacement of six leader sequences, corresponding to regions of HCV polyprotein that are cleaved by NS3. The large numbers of potential 14-mer and 16-mer peptide inhibitors thus obtained were tested against NS3 using the fluorescent probe RETS1 and peptide cofactor SVVIVGRIILSGRA from NS4A protein. This afforded several peptide inhibitors with an IC50 of around 2 μM. These peptides may be good leading compounds for the development of peptidomimetics to control HCV replication in the treatment of chronic hepatitis C.</description><subject>Amino Acid Sequence</subject><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>Antiviral agents</subject><subject>Antiviral Agents - chemistry</subject><subject>Antiviral Agents - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Fluorescent indicators</subject><subject>Hepatitis</subject><subject>Hepatitis C</subject><subject>Hepatitis C - drug therapy</subject><subject>Hepatitis C virus</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>Inhibitory Concentration 50</subject><subject>Interferon</subject><subject>Kinetics</subject><subject>Medical sciences</subject><subject>Molecular Mimicry</subject><subject>NS4A protein</subject><subject>Oligopeptides - chemistry</subject><subject>Oligopeptides - pharmacology</subject><subject>Peptide inhibitors</subject><subject>Peptides</subject><subject>Peptidomimetics</subject><subject>Pharmacology. Drug treatments</subject><subject>Protease Inhibitors - chemistry</subject><subject>Protease Inhibitors - pharmacology</subject><subject>Protein sorting signals</subject><subject>Proteinase</subject><subject>Replication</subject><subject>Structure-Activity Relationship</subject><subject>Viral Nonstructural Proteins - antagonists & inhibitors</subject><issn>2040-2066</issn><issn>0956-3202</issn><issn>2040-2066</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp90MtKw0AUBuBBFFurL-BCAqK72DP3maUUtQXRgpdtmEwmOiVN6kyy8O2NNFBRcHXO4jsXfoROMVxhLOUUNBeUAAEKmAFwwHtoTIBBSkCI_R_9CB3FuAKgilN9iEaYCc204mPElm7T-sIli_rd575tQkyaMpm7jWl962MyS1596GLy8ESTZWhaZ6I7RgelqaI7GeoEvdzePM_m6f3j3WJ2fZ9aqiROVWmVtJIybaVUjuUFFlZgy7gp8twZLVVe5qCotUpLIkphmWIgCRXGaSfoBF1u925C89G52GZrH62rKlO7posZVkAU1biH57_gqulC3f-WEcoI5QyE6hXZKhuaGIMrs03waxM-MwzZd6LZ30T7obNhdZevXbEbGSLswcUATLSmKoOprY87xynhXEHvplsXzZvb_ffP6S9TnIeW</recordid><startdate>200310</startdate><enddate>200310</enddate><creator>Portal-Núñez, Sergio</creator><creator>González-Navarro, Carlos J</creator><creator>García-Delgado, Marina</creator><creator>Vizmanos, José Luis</creator><creator>Lasarte, Juan José</creator><creator>Borrás-Cuesta, Francisco</creator><general>SAGE Publications</general><general>International Medical Press</general><general>Sage Publications Ltd</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T5</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7U9</scope></search><sort><creationdate>200310</creationdate><title>Peptide Inhibitors of Hepatitis C Virus NS3 Protease</title><author>Portal-Núñez, Sergio ; González-Navarro, Carlos J ; García-Delgado, Marina ; Vizmanos, José Luis ; Lasarte, Juan José ; Borrás-Cuesta, Francisco</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3871-8fc87c7349c778e4bd16c61c45adbbea978bfb083cc89726f6c48407236ae9e63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Antibiotics. Antiinfectious agents. Antiparasitic agents</topic><topic>Antiviral agents</topic><topic>Antiviral Agents - chemistry</topic><topic>Antiviral Agents - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Fluorescent indicators</topic><topic>Hepatitis</topic><topic>Hepatitis C</topic><topic>Hepatitis C - drug therapy</topic><topic>Hepatitis C virus</topic><topic>Humans</topic><topic>Hydrolysis</topic><topic>Inhibitory Concentration 50</topic><topic>Interferon</topic><topic>Kinetics</topic><topic>Medical sciences</topic><topic>Molecular Mimicry</topic><topic>NS4A protein</topic><topic>Oligopeptides - chemistry</topic><topic>Oligopeptides - pharmacology</topic><topic>Peptide inhibitors</topic><topic>Peptides</topic><topic>Peptidomimetics</topic><topic>Pharmacology. Drug treatments</topic><topic>Protease Inhibitors - chemistry</topic><topic>Protease Inhibitors - pharmacology</topic><topic>Protein sorting signals</topic><topic>Proteinase</topic><topic>Replication</topic><topic>Structure-Activity Relationship</topic><topic>Viral Nonstructural Proteins - antagonists & inhibitors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Portal-Núñez, Sergio</creatorcontrib><creatorcontrib>González-Navarro, Carlos J</creatorcontrib><creatorcontrib>García-Delgado, Marina</creatorcontrib><creatorcontrib>Vizmanos, José Luis</creatorcontrib><creatorcontrib>Lasarte, Juan José</creatorcontrib><creatorcontrib>Borrás-Cuesta, Francisco</creatorcontrib><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>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Virology and AIDS Abstracts</collection><jtitle>Antiviral chemistry & chemotherapy</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Portal-Núñez, Sergio</au><au>González-Navarro, Carlos J</au><au>García-Delgado, Marina</au><au>Vizmanos, José Luis</au><au>Lasarte, Juan José</au><au>Borrás-Cuesta, Francisco</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Peptide Inhibitors of Hepatitis C Virus NS3 Protease</atitle><jtitle>Antiviral chemistry & chemotherapy</jtitle><addtitle>Antivir Chem Chemother</addtitle><date>2003-10</date><risdate>2003</risdate><volume>14</volume><issue>5</issue><spage>225</spage><epage>233</epage><pages>225-233</pages><issn>2040-2066</issn><issn>0956-3202</issn><eissn>2040-2066</eissn><abstract>Hepatitis C virus (HCV) is a highly prevalent virus and one of the major agents of chronic hepatitis. Since HCV NS3 protease is essential for the processing of HCV polyprotein, this protease is a target of choice to control HCV replication. Peptide inhibitors of NS3 were developed by selective amino acid replacement of six leader sequences, corresponding to regions of HCV polyprotein that are cleaved by NS3. The large numbers of potential 14-mer and 16-mer peptide inhibitors thus obtained were tested against NS3 using the fluorescent probe RETS1 and peptide cofactor SVVIVGRIILSGRA from NS4A protein. This afforded several peptide inhibitors with an IC50 of around 2 μM. These peptides may be good leading compounds for the development of peptidomimetics to control HCV replication in the treatment of chronic hepatitis C.</abstract><cop>London, England</cop><pub>SAGE Publications</pub><pmid>14694985</pmid><doi>10.1177/095632020301400501</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Antibiotics. Antiinfectious agents. Antiparasitic agents Antiviral agents Antiviral Agents - chemistry Antiviral Agents - pharmacology Biological and medical sciences Fluorescent indicators Hepatitis Hepatitis C Hepatitis C - drug therapy Hepatitis C virus Humans Hydrolysis Inhibitory Concentration 50 Interferon Kinetics Medical sciences Molecular Mimicry NS4A protein Oligopeptides - chemistry Oligopeptides - pharmacology Peptide inhibitors Peptides Peptidomimetics Pharmacology. Drug treatments Protease Inhibitors - chemistry Protease Inhibitors - pharmacology Protein sorting signals Proteinase Replication Structure-Activity Relationship Viral Nonstructural Proteins - antagonists & inhibitors |
| title | Peptide Inhibitors of Hepatitis C Virus NS3 Protease |
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