SrasV1, Main, Exploration, bibRecord, 006469

Inhibition of hepatitis C virus NS3 protease activity by product-based peptides is dependent on helicase domain

Identifieur interne : 006469 ( Main/Exploration ); précédent : 006468; suivant : 006470

Inhibition of hepatitis C virus NS3 protease activity by product-based peptides is dependent on helicase domain

Auteurs : Anja Johansson [Suède] ; Ina Hubatsch [Suède] ; Eva Akerblom [Suède] ; Gunnar Lindeberg [Suède] ; Susanne Winiwarter [Suède] ; U. Helena Danielson [Suède] ; Anders Hallberg [Suède]

Source :

Bioorganic & medicinal chemistry letters [ 0960-894X ] ; 2001.

RBID : Pascal:01-0123478

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.
Pascal (Inist)
- Cinétique, Fragments peptidiques, Protéines de liaison à l'ADN, Relation structure activité, Antiviral, Relation structure-activité, Structure tertiaire des protéines, Virus hépatite C, Inhibiteur enzyme, Peptidases, Domaine moléculaire, In vitro, Synthèse chimique, Synthèse peptidique, Phase solide, Peptide soufre, Hexapeptide, Modification chimique, NS3 protease, Alanine(3,3-diphényl), Glutamique acide(γ-carboxy), β-Cyclohexylalanine.

English descriptors

KwdEn :
- Antiviral, Chemical modification, Chemical synthesis, DNA-Binding Proteins (chemistry), Enzyme inhibitor, Hepacivirus (enzymology), Hepatitis C virus, Hexapeptide, In vitro, Kinetics, Molecular domain, Peptidases, Peptide Fragments (chemical synthesis), Peptide Fragments (chemistry), Peptide Fragments (pharmacology), Peptide synthesis, Protein Structure, Tertiary, Serine Proteinase Inhibitors (chemical synthesis), Serine Proteinase Inhibitors (pharmacology), Solid phase, Structure activity relation, Structure-Activity Relationship, Sulfur peptide, 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.

Affiliations:

Le document en format XML

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<term>Chemical modification</term>
<term>Chemical synthesis</term>
<term>DNA-Binding Proteins (chemistry)</term>
<term>Enzyme inhibitor</term>
<term>Hepacivirus (enzymology)</term>
<term>Hepatitis C virus</term>
<term>Hexapeptide</term>
<term>In vitro</term>
<term>Kinetics</term>
<term>Molecular domain</term>
<term>Peptidases</term>
<term>Peptide Fragments (chemical synthesis)</term>
<term>Peptide Fragments (chemistry)</term>
<term>Peptide Fragments (pharmacology)</term>
<term>Peptide synthesis</term>
<term>Protein Structure, Tertiary</term>
<term>Serine Proteinase Inhibitors (chemical synthesis)</term>
<term>Serine Proteinase Inhibitors (pharmacology)</term>
<term>Solid phase</term>
<term>Structure activity relation</term>
<term>Structure-Activity Relationship</term>
<term>Sulfur peptide</term>
<term>Viral Nonstructural Proteins (antagonists & inhibitors)</term>
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<term>Fragments peptidiques ()</term>
<term>Fragments peptidiques (pharmacologie)</term>
<term>Fragments peptidiques (synthèse chimique)</term>
<term>Hepacivirus (enzymologie)</term>
<term>Inhibiteurs de la sérine protéinase (pharmacologie)</term>
<term>Inhibiteurs de la sérine protéinase (synthèse chimique)</term>
<term>Protéines de liaison à l'ADN ()</term>
<term>Protéines virales non structurales (antagonistes et inhibiteurs)</term>
<term>Relation structure-activité</term>
<term>Structure tertiaire des protéines</term>
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<term>Serine Proteinase Inhibitors</term>
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<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Fragments peptidiques</term>
<term>Inhibiteurs de la sérine protéinase</term>
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<term>Inhibiteurs de la sérine protéinase</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Kinetics</term>
<term>Protein Structure, Tertiary</term>
<term>Structure-Activity Relationship</term>
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<term>Fragments peptidiques</term>
<term>Protéines de liaison à l'ADN</term>
<term>Relation structure activité</term>
<term>Antiviral</term>
<term>Relation structure-activité</term>
<term>Structure tertiaire des protéines</term>
<term>Virus hépatite C</term>
<term>Inhibiteur enzyme</term>
<term>Peptidases</term>
<term>Domaine moléculaire</term>
<term>In vitro</term>
<term>Synthèse chimique</term>
<term>Synthèse peptidique</term>
<term>Phase solide</term>
<term>Peptide soufre</term>
<term>Hexapeptide</term>
<term>Modification chimique</term>
<term>NS3 protease</term>
<term>Alanine(3,3-diphényl)</term>
<term>Glutamique acide(γ-carboxy)</term>
<term>β-Cyclohexylalanine</term>
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<front><div type="abstract" xml:lang="en">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.</div>
</front>
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<name sortKey="Hallberg, Anders" sort="Hallberg, Anders" uniqKey="Hallberg A" first="Anders" last="Hallberg">Anders Hallberg</name>
<name sortKey="Hubatsch, Ina" sort="Hubatsch, Ina" uniqKey="Hubatsch I" first="Ina" last="Hubatsch">Ina Hubatsch</name>
<name sortKey="Lindeberg, Gunnar" sort="Lindeberg, Gunnar" uniqKey="Lindeberg G" first="Gunnar" last="Lindeberg">Gunnar Lindeberg</name>
<name sortKey="Winiwarter, Susanne" sort="Winiwarter, Susanne" uniqKey="Winiwarter S" first="Susanne" last="Winiwarter">Susanne Winiwarter</name>
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   |wiki=    Sante
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   |clé=     Pascal:01-0123478
   |texte=   Inhibition of hepatitis C virus NS3 protease activity by product-based peptides is dependent on helicase domain
}}

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Inhibition of hepatitis C virus NS3 protease activity by product-based peptides is dependent on helicase domain

Inhibition of hepatitis C virus NS3 protease activity by product-based peptides is dependent on helicase domain

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