Loading…
Studies on the C-terminal of hexapeptide inhibitors of the hepatitis C virus serine protease
Replacememt of the C-terminal carboxylic acid functionality of peptide inhibitors of hepatitis C virus (HCV) NS3 protease (complexed with NS4A peptide cofactor) by activated carbonyl groups does not produce any substantial increase in potency. These latter inhibitors also inhibit a variety of other...
Saved in:
| Published in: | Bioorganic & medicinal chemistry letters 1998-10, Vol.8 (19), p.2719-2724 |
|---|---|
| Main Authors: | , , , , , , , , , , , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c389t-98805c79085d71bda44294cf499fda650294ea0ca6504cb0b7de9a643fd0cb683 |
|---|---|
| cites | cdi_FETCH-LOGICAL-c389t-98805c79085d71bda44294cf499fda650294ea0ca6504cb0b7de9a643fd0cb683 |
| container_end_page | 2724 |
| container_issue | 19 |
| container_start_page | 2719 |
| container_title | Bioorganic & medicinal chemistry letters |
| container_volume | 8 |
| creator | Llinàs-Brunet, Montse Bailey, Murray Déziel, Robert Fazal, Gulrez Gorys, Vida Goulet, Sylvie Halmos, Ted Maurice, Roger Poirier, Martin Poupart, Marc-André Rancourt, Jean Thibeault, Diane Wernic, Dominik Lamarre, Daniel |
| description | Replacememt of the C-terminal carboxylic acid functionality of peptide inhibitors of hepatitis C virus (HCV) NS3 protease (complexed with NS4A peptide cofactor) by activated carbonyl groups does not produce any substantial increase in potency. These latter inhibitors also inhibit a variety of other serine and cysteine proteases whereas the carboxylic acids are specific. Norvaline was identified as a chemically stable replacement for the P1 residue of Ac-DDIVPC-OH which was also compatible with activated carbonyl functionalities. |
| doi_str_mv | 10.1016/S0960-894X(98)00480-6 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_69112668</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0960894X98004806</els_id><sourcerecordid>69112668</sourcerecordid><originalsourceid>FETCH-LOGICAL-c389t-98805c79085d71bda44294cf499fda650294ea0ca6504cb0b7de9a643fd0cb683</originalsourceid><addsrcrecordid>eNqFkE1r3DAQhkVJSLdpf0JAhxLag5PRWtZKpxCWfBQCPaSFHgpClsasitd2NHJo_33s3WWvPWnE-8wHD2MXAq4ECHX9DEZBoY389cXorwBSQ6HesYWQShalhOqELY7Ie_aB6A-AkCDlGTszelUqAQv2-zmPISLxvuN5g3xdZEzb2LmW9w3f4F834JBjQB67Taxj7hPNycxucHA55kh8zV9jGokTptghH1Kf0RF-ZKeNawk_Hd5z9vP-7sf6sXj6_vBtfftU-FKbXBitofIrA7oKK1EHJ-XSSN9IY5rgVAXTDx34uZS-hnoV0DglyyaAr5Uuz9nlfu60-GVEynYbyWPbug77kawyQizVDqz2oE89UcLGDiluXfpnBdjZqt1ZtbMya7TdWbVq6rs4LBjrLYZj10HjlH8-5I68a5vkOh_piC3lUpbVjN3sMZxkvEZMlnzEzmOICX22oY__OeQNhJmUtA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>69112668</pqid></control><display><type>article</type><title>Studies on the C-terminal of hexapeptide inhibitors of the hepatitis C virus serine protease</title><source>ScienceDirect Journals</source><creator>Llinàs-Brunet, Montse ; Bailey, Murray ; Déziel, Robert ; Fazal, Gulrez ; Gorys, Vida ; Goulet, Sylvie ; Halmos, Ted ; Maurice, Roger ; Poirier, Martin ; Poupart, Marc-André ; Rancourt, Jean ; Thibeault, Diane ; Wernic, Dominik ; Lamarre, Daniel</creator><creatorcontrib>Llinàs-Brunet, Montse ; Bailey, Murray ; Déziel, Robert ; Fazal, Gulrez ; Gorys, Vida ; Goulet, Sylvie ; Halmos, Ted ; Maurice, Roger ; Poirier, Martin ; Poupart, Marc-André ; Rancourt, Jean ; Thibeault, Diane ; Wernic, Dominik ; Lamarre, Daniel</creatorcontrib><description>Replacememt of the C-terminal carboxylic acid functionality of peptide inhibitors of hepatitis C virus (HCV) NS3 protease (complexed with NS4A peptide cofactor) by activated carbonyl groups does not produce any substantial increase in potency. These latter inhibitors also inhibit a variety of other serine and cysteine proteases whereas the carboxylic acids are specific. Norvaline was identified as a chemically stable replacement for the P1 residue of Ac-DDIVPC-OH which was also compatible with activated carbonyl functionalities.</description><identifier>ISSN: 0960-894X</identifier><identifier>EISSN: 1464-3405</identifier><identifier>DOI: 10.1016/S0960-894X(98)00480-6</identifier><identifier>PMID: 9873610</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents ; Antiviral agents ; Biological and medical sciences ; Cysteine - chemistry ; Cysteine - pharmacology ; Hepacivirus - enzymology ; Medical sciences ; Oligopeptides - chemical synthesis ; Oligopeptides - pharmacology ; Pharmacology. Drug treatments ; Serine Proteinase Inhibitors - chemical synthesis ; Serine Proteinase Inhibitors - pharmacology ; Structure-Activity Relationship ; Viral Nonstructural Proteins - antagonists & inhibitors</subject><ispartof>Bioorganic & medicinal chemistry letters, 1998-10, Vol.8 (19), p.2719-2724</ispartof><rights>1998</rights><rights>1998 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c389t-98805c79085d71bda44294cf499fda650294ea0ca6504cb0b7de9a643fd0cb683</citedby><cites>FETCH-LOGICAL-c389t-98805c79085d71bda44294cf499fda650294ea0ca6504cb0b7de9a643fd0cb683</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2424350$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9873610$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Llinàs-Brunet, Montse</creatorcontrib><creatorcontrib>Bailey, Murray</creatorcontrib><creatorcontrib>Déziel, Robert</creatorcontrib><creatorcontrib>Fazal, Gulrez</creatorcontrib><creatorcontrib>Gorys, Vida</creatorcontrib><creatorcontrib>Goulet, Sylvie</creatorcontrib><creatorcontrib>Halmos, Ted</creatorcontrib><creatorcontrib>Maurice, Roger</creatorcontrib><creatorcontrib>Poirier, Martin</creatorcontrib><creatorcontrib>Poupart, Marc-André</creatorcontrib><creatorcontrib>Rancourt, Jean</creatorcontrib><creatorcontrib>Thibeault, Diane</creatorcontrib><creatorcontrib>Wernic, Dominik</creatorcontrib><creatorcontrib>Lamarre, Daniel</creatorcontrib><title>Studies on the C-terminal of hexapeptide inhibitors of the hepatitis C virus serine protease</title><title>Bioorganic & medicinal chemistry letters</title><addtitle>Bioorg Med Chem Lett</addtitle><description>Replacememt of the C-terminal carboxylic acid functionality of peptide inhibitors of hepatitis C virus (HCV) NS3 protease (complexed with NS4A peptide cofactor) by activated carbonyl groups does not produce any substantial increase in potency. These latter inhibitors also inhibit a variety of other serine and cysteine proteases whereas the carboxylic acids are specific. Norvaline was identified as a chemically stable replacement for the P1 residue of Ac-DDIVPC-OH which was also compatible with activated carbonyl functionalities.</description><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>Antiviral agents</subject><subject>Biological and medical sciences</subject><subject>Cysteine - chemistry</subject><subject>Cysteine - pharmacology</subject><subject>Hepacivirus - enzymology</subject><subject>Medical sciences</subject><subject>Oligopeptides - chemical synthesis</subject><subject>Oligopeptides - pharmacology</subject><subject>Pharmacology. Drug treatments</subject><subject>Serine Proteinase Inhibitors - chemical synthesis</subject><subject>Serine Proteinase Inhibitors - pharmacology</subject><subject>Structure-Activity Relationship</subject><subject>Viral Nonstructural Proteins - antagonists & inhibitors</subject><issn>0960-894X</issn><issn>1464-3405</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNqFkE1r3DAQhkVJSLdpf0JAhxLag5PRWtZKpxCWfBQCPaSFHgpClsasitd2NHJo_33s3WWvPWnE-8wHD2MXAq4ECHX9DEZBoY389cXorwBSQ6HesYWQShalhOqELY7Ie_aB6A-AkCDlGTszelUqAQv2-zmPISLxvuN5g3xdZEzb2LmW9w3f4F834JBjQB67Taxj7hPNycxucHA55kh8zV9jGokTptghH1Kf0RF-ZKeNawk_Hd5z9vP-7sf6sXj6_vBtfftU-FKbXBitofIrA7oKK1EHJ-XSSN9IY5rgVAXTDx34uZS-hnoV0DglyyaAr5Uuz9nlfu60-GVEynYbyWPbug77kawyQizVDqz2oE89UcLGDiluXfpnBdjZqt1ZtbMya7TdWbVq6rs4LBjrLYZj10HjlH8-5I68a5vkOh_piC3lUpbVjN3sMZxkvEZMlnzEzmOICX22oY__OeQNhJmUtA</recordid><startdate>19981006</startdate><enddate>19981006</enddate><creator>Llinàs-Brunet, Montse</creator><creator>Bailey, Murray</creator><creator>Déziel, Robert</creator><creator>Fazal, Gulrez</creator><creator>Gorys, Vida</creator><creator>Goulet, Sylvie</creator><creator>Halmos, Ted</creator><creator>Maurice, Roger</creator><creator>Poirier, Martin</creator><creator>Poupart, Marc-André</creator><creator>Rancourt, Jean</creator><creator>Thibeault, Diane</creator><creator>Wernic, Dominik</creator><creator>Lamarre, Daniel</creator><general>Elsevier Ltd</general><general>Elsevier</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>7X8</scope></search><sort><creationdate>19981006</creationdate><title>Studies on the C-terminal of hexapeptide inhibitors of the hepatitis C virus serine protease</title><author>Llinàs-Brunet, Montse ; Bailey, Murray ; Déziel, Robert ; Fazal, Gulrez ; Gorys, Vida ; Goulet, Sylvie ; Halmos, Ted ; Maurice, Roger ; Poirier, Martin ; Poupart, Marc-André ; Rancourt, Jean ; Thibeault, Diane ; Wernic, Dominik ; Lamarre, Daniel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-98805c79085d71bda44294cf499fda650294ea0ca6504cb0b7de9a643fd0cb683</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Antibiotics. Antiinfectious agents. Antiparasitic agents</topic><topic>Antiviral agents</topic><topic>Biological and medical sciences</topic><topic>Cysteine - chemistry</topic><topic>Cysteine - pharmacology</topic><topic>Hepacivirus - enzymology</topic><topic>Medical sciences</topic><topic>Oligopeptides - chemical synthesis</topic><topic>Oligopeptides - pharmacology</topic><topic>Pharmacology. Drug treatments</topic><topic>Serine Proteinase Inhibitors - chemical synthesis</topic><topic>Serine Proteinase Inhibitors - pharmacology</topic><topic>Structure-Activity Relationship</topic><topic>Viral Nonstructural Proteins - antagonists & inhibitors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Llinàs-Brunet, Montse</creatorcontrib><creatorcontrib>Bailey, Murray</creatorcontrib><creatorcontrib>Déziel, Robert</creatorcontrib><creatorcontrib>Fazal, Gulrez</creatorcontrib><creatorcontrib>Gorys, Vida</creatorcontrib><creatorcontrib>Goulet, Sylvie</creatorcontrib><creatorcontrib>Halmos, Ted</creatorcontrib><creatorcontrib>Maurice, Roger</creatorcontrib><creatorcontrib>Poirier, Martin</creatorcontrib><creatorcontrib>Poupart, Marc-André</creatorcontrib><creatorcontrib>Rancourt, Jean</creatorcontrib><creatorcontrib>Thibeault, Diane</creatorcontrib><creatorcontrib>Wernic, Dominik</creatorcontrib><creatorcontrib>Lamarre, Daniel</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>MEDLINE - Academic</collection><jtitle>Bioorganic & medicinal chemistry letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Llinàs-Brunet, Montse</au><au>Bailey, Murray</au><au>Déziel, Robert</au><au>Fazal, Gulrez</au><au>Gorys, Vida</au><au>Goulet, Sylvie</au><au>Halmos, Ted</au><au>Maurice, Roger</au><au>Poirier, Martin</au><au>Poupart, Marc-André</au><au>Rancourt, Jean</au><au>Thibeault, Diane</au><au>Wernic, Dominik</au><au>Lamarre, Daniel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Studies on the C-terminal of hexapeptide inhibitors of the hepatitis C virus serine protease</atitle><jtitle>Bioorganic & medicinal chemistry letters</jtitle><addtitle>Bioorg Med Chem Lett</addtitle><date>1998-10-06</date><risdate>1998</risdate><volume>8</volume><issue>19</issue><spage>2719</spage><epage>2724</epage><pages>2719-2724</pages><issn>0960-894X</issn><eissn>1464-3405</eissn><abstract>Replacememt of the C-terminal carboxylic acid functionality of peptide inhibitors of hepatitis C virus (HCV) NS3 protease (complexed with NS4A peptide cofactor) by activated carbonyl groups does not produce any substantial increase in potency. These latter inhibitors also inhibit a variety of other serine and cysteine proteases whereas the carboxylic acids are specific. Norvaline was identified as a chemically stable replacement for the P1 residue of Ac-DDIVPC-OH which was also compatible with activated carbonyl functionalities.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>9873610</pmid><doi>10.1016/S0960-894X(98)00480-6</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0960-894X |
| ispartof | Bioorganic & medicinal chemistry letters, 1998-10, Vol.8 (19), p.2719-2724 |
| issn | 0960-894X 1464-3405 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_69112668 |
| source | ScienceDirect Journals |
| subjects | Antibiotics. Antiinfectious agents. Antiparasitic agents Antiviral agents Biological and medical sciences Cysteine - chemistry Cysteine - pharmacology Hepacivirus - enzymology Medical sciences Oligopeptides - chemical synthesis Oligopeptides - pharmacology Pharmacology. Drug treatments Serine Proteinase Inhibitors - chemical synthesis Serine Proteinase Inhibitors - pharmacology Structure-Activity Relationship Viral Nonstructural Proteins - antagonists & inhibitors |
| title | Studies on the C-terminal of hexapeptide inhibitors of the hepatitis C virus serine protease |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T21%3A45%3A49IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Studies%20on%20the%20C-terminal%20of%20hexapeptide%20inhibitors%20of%20the%20hepatitis%20C%20virus%20serine%20protease&rft.jtitle=Bioorganic%20&%20medicinal%20chemistry%20letters&rft.au=Llin%C3%A0s-Brunet,%20Montse&rft.date=1998-10-06&rft.volume=8&rft.issue=19&rft.spage=2719&rft.epage=2724&rft.pages=2719-2724&rft.issn=0960-894X&rft.eissn=1464-3405&rft_id=info:doi/10.1016/S0960-894X(98)00480-6&rft_dat=%3Cproquest_cross%3E69112668%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c389t-98805c79085d71bda44294cf499fda650294ea0ca6504cb0b7de9a643fd0cb683%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=69112668&rft_id=info:pmid/9873610&rfr_iscdi=true |