Inhibition of hepatitis C virus NS3 protease activity by product-based peptides is dependent on helicase domain.
Identifieur interne : 000010 ( Ncbi/Merge ); précédent : 000009; suivant : 000011Inhibition of hepatitis C virus NS3 protease activity by product-based peptides is dependent on helicase domain.
Auteurs : A. Johansson [Suède] ; I. Hubatsch ; E. Akerblom ; G. Lindeberg ; S. Winiwarter ; U H Danielson ; A. HallbergSource :
- Bioorganic & medicinal chemistry letters [ 0960-894X ] ; 2001.
Descripteurs français
- KwdFr :
- Cinétique, Fragments peptidiques (), Fragments peptidiques (pharmacologie), Fragments peptidiques (synthèse chimique), Hepacivirus (enzymologie), Inhibiteurs de la sérine protéinase (pharmacologie), Inhibiteurs de la sérine protéinase (synthèse chimique), Protéines de liaison à l'ADN (), Protéines virales non structurales (antagonistes et inhibiteurs), Relation structure-activité, Structure tertiaire des protéines.
- MESH :
- antagonistes et inhibiteurs : Protéines virales non structurales.
- enzymologie : Hepacivirus.
- pharmacologie : Fragments peptidiques, Inhibiteurs de la sérine protéinase.
- synthèse chimique : Fragments peptidiques, Inhibiteurs de la sérine protéinase.
- Cinétique, Fragments peptidiques, Protéines de liaison à l'ADN, Relation structure-activité, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- DNA-Binding Proteins (chemistry), Hepacivirus (enzymology), Kinetics, Peptide Fragments (chemical synthesis), Peptide Fragments (chemistry), Peptide Fragments (pharmacology), Protein Structure, Tertiary, Serine Proteinase Inhibitors (chemical synthesis), Serine Proteinase Inhibitors (pharmacology), Structure-Activity Relationship, Viral Nonstructural Proteins (antagonists & inhibitors).
- MESH :
- chemical , antagonists & inhibitors : Viral Nonstructural Proteins.
- chemical , chemical synthesis : Peptide Fragments, Serine Proteinase Inhibitors.
- chemical , chemistry : DNA-Binding Proteins, Peptide Fragments.
- enzymology : Hepacivirus.
- chemical , pharmacology : Peptide Fragments, Serine Proteinase Inhibitors.
- Kinetics, Protein Structure, Tertiary, Structure-Activity Relationship.
Abstract
Structure activity relationships (SARs) of product-based inhibitors of hepatitis C virus NS3 protease were evaluated using an in vitro assay system comprising the native bifunctional full-length NS3 (protease-helicase/NTPase). The results were compared to previously reported data derived from the corresponding NS3 protease domain assay. Shortening the length of the protease inhibitors from hexapeptides to tripeptides revealed that the decrease in potency was much less when determined in the assay system with the full-length NS3 protein. Disagreements in SARs at different positions (P5 P2) were also discovered. Taken together, the results suggest that the impact of the helicase domain upon protease inhibitor binding is substantial.
DOI: 10.1016/s0960-894x(00)00625-9
PubMed: 11206459
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The results were compared to previously reported data derived from the corresponding NS3 protease domain assay. Shortening the length of the protease inhibitors from hexapeptides to tripeptides revealed that the decrease in potency was much less when determined in the assay system with the full-length NS3 protein. Disagreements in SARs at different positions (P5 P2) were also discovered. Taken together, the results suggest that the impact of the helicase domain upon protease inhibitor binding is substantial.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11206459</PMID><DateCompleted><Year>2001</Year><Month>05</Month><Day>10</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>19</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0960-894X</ISSN><JournalIssue CitedMedium="Print"><Volume>11</Volume><Issue>2</Issue><PubDate><Year>2001</Year><Month>Jan</Month><Day>22</Day></PubDate></JournalIssue><Title>Bioorganic & medicinal chemistry letters</Title><ISOAbbreviation>Bioorg. Med. Chem. Lett.</ISOAbbreviation></Journal><ArticleTitle>Inhibition of hepatitis C virus NS3 protease activity by product-based peptides is dependent on helicase domain.</ArticleTitle><Pagination><MedlinePgn>203-6</MedlinePgn></Pagination><Abstract><AbstractText>Structure activity relationships (SARs) of product-based inhibitors of hepatitis C virus NS3 protease were evaluated using an in vitro assay system comprising the native bifunctional full-length NS3 (protease-helicase/NTPase). The results were compared to previously reported data derived from the corresponding NS3 protease domain assay. Shortening the length of the protease inhibitors from hexapeptides to tripeptides revealed that the decrease in potency was much less when determined in the assay system with the full-length NS3 protein. Disagreements in SARs at different positions (P5 P2) were also discovered. Taken together, the results suggest that the impact of the helicase domain upon protease inhibitor binding is substantial.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Johansson</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Organic Pharmaceutical Chemistry, Uppsala University, BMC, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hubatsch</LastName><ForeName>I</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Akerblom</LastName><ForeName>E</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Lindeberg</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Winiwarter</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Danielson</LastName><ForeName>U H</ForeName><Initials>UH</Initials></Author><Author ValidYN="Y"><LastName>Hallberg</LastName><ForeName>A</ForeName><Initials>A</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Bioorg Med Chem Lett</MedlineTA><NlmUniqueID>9107377</NlmUniqueID><ISSNLinking>0960-894X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004268">DNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C084422">NS3 protein, hepatitis C virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015842">Serine Proteinase Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016174" MajorTopicYN="N">Hepacivirus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010446" MajorTopicYN="N">Peptide Fragments</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015842" MajorTopicYN="N">Serine Proteinase Inhibitors</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="Y">chemical synthesis</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017361" MajorTopicYN="N">Viral Nonstructural Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2001</Year><Month>2</Month><Day>24</Day><Hour>12</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>5</Month><Day>22</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2001</Year><Month>2</Month><Day>24</Day><Hour>12</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11206459</ArticleId><ArticleId IdType="pii">S0960894X00006259</ArticleId><ArticleId IdType="doi">10.1016/s0960-894x(00)00625-9</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country><region><li>East Middle Sweden</li><li>Svealand</li></region><settlement><li>Uppsala</li></settlement><orgName><li>Université d'Uppsala</li></orgName></list><tree><noCountry><name sortKey="Akerblom, E" sort="Akerblom, E" uniqKey="Akerblom E" first="E" last="Akerblom">E. Akerblom</name><name sortKey="Danielson, U H" sort="Danielson, U H" uniqKey="Danielson U" first="U H" last="Danielson">U H Danielson</name><name sortKey="Hallberg, A" sort="Hallberg, A" uniqKey="Hallberg A" first="A" last="Hallberg">A. Hallberg</name><name sortKey="Hubatsch, I" sort="Hubatsch, I" uniqKey="Hubatsch I" first="I" last="Hubatsch">I. Hubatsch</name><name sortKey="Lindeberg, G" sort="Lindeberg, G" uniqKey="Lindeberg G" first="G" last="Lindeberg">G. Lindeberg</name><name sortKey="Winiwarter, S" sort="Winiwarter, S" uniqKey="Winiwarter S" first="S" last="Winiwarter">S. Winiwarter</name></noCountry><country name="Suède"><region name="Svealand"><name sortKey="Johansson, A" sort="Johansson, A" uniqKey="Johansson A" first="A" last="Johansson">A. Johansson</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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