SrasV1, PubMed, Checkpoint, bibRecord, 001199

Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: structure-activity relationship study.

Identifieur interne : 001199 ( PubMed/Checkpoint ); précédent : 001198; suivant : 001200

Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: structure-activity relationship study.

Auteurs : Pillaiyar Thanigaimalai [Japon] ; Sho Konno ; Takehito Yamamoto ; Yuji Koiwai ; Akihiro Taguchi ; Kentaro Takayama ; Fumika Yakushiji ; Kenichi Akaji ; Yoshiaki Kiso ; Yuko Kawasaki ; Shen-En Chen ; Aurash Naser-Tavakolian ; Arne Schön ; Ernesto Freire ; Yoshio Hayashi

Source :

European journal of medicinal chemistry [ 1768-3254 ] ; 2013.

RBID : pubmed:23747811

Descripteurs français

KwdFr :
- Conception de médicament, Conformation moléculaire, Cysteine endopeptidases (métabolisme), Dipeptides (), Dipeptides (pharmacologie), Dipeptides (synthèse chimique), Humains, Inhibiteurs de la cystéine protéinase (), Inhibiteurs de la cystéine protéinase (pharmacologie), Inhibiteurs de la cystéine protéinase (synthèse chimique), Masse moléculaire, Modèles moléculaires, Protéines virales (antagonistes et inhibiteurs), Protéines virales (métabolisme), Relation dose-effet des médicaments, Relation structure-activité, Virus du SRAS (), Virus du SRAS (enzymologie).
MESH :
- antagonistes et inhibiteurs : Protéines virales.
- enzymologie : Virus du SRAS.
- métabolisme : Cysteine endopeptidases, Protéines virales.
- pharmacologie : Dipeptides, Inhibiteurs de la cystéine protéinase.
- synthèse chimique : Dipeptides, Inhibiteurs de la cystéine protéinase.
- Conception de médicament, Conformation moléculaire, Dipeptides, Humains, Inhibiteurs de la cystéine protéinase, Masse moléculaire, Modèles moléculaires, Relation dose-effet des médicaments, Relation structure-activité, Virus du SRAS.

English descriptors

KwdEn :
- Cysteine Endopeptidases (metabolism), Cysteine Proteinase Inhibitors (chemical synthesis), Cysteine Proteinase Inhibitors (chemistry), Cysteine Proteinase Inhibitors (pharmacology), Dipeptides (chemical synthesis), Dipeptides (chemistry), Dipeptides (pharmacology), Dose-Response Relationship, Drug, Drug Design, Humans, Models, Molecular, Molecular Conformation, Molecular Weight, SARS Virus (drug effects), SARS Virus (enzymology), Structure-Activity Relationship, Viral Proteins (antagonists & inhibitors), Viral Proteins (metabolism).
MESH :
- chemical , antagonists & inhibitors : Viral Proteins.
- chemical , chemical synthesis : Cysteine Proteinase Inhibitors, Dipeptides.
- chemical , chemistry : Cysteine Proteinase Inhibitors, Dipeptides.
- chemical , metabolism : Cysteine Endopeptidases, Viral Proteins.
- chemical , pharmacology : Cysteine Proteinase Inhibitors, Dipeptides.
- drug effects : SARS Virus.
- enzymology : SARS Virus.
- Dose-Response Relationship, Drug, Drug Design, Humans, Models, Molecular, Molecular Conformation, Molecular Weight, Structure-Activity Relationship.

Abstract

This work describes the design, synthesis, and evaluation of low-molecular weight peptidic SARS-CoV 3CL protease inhibitors. The inhibitors were designed based on the potent tripeptidic Z-Val-Leu-Ala(pyrrolidone-3-yl)-2-benzothiazole (8; Ki = 4.1 nM), in which the P3 valine unit was substituted with a variety of distinct moieties. The resulting series of dipeptide-type inhibitors displayed moderate to good inhibitory activities against 3CL(pro). In particular, compounds 26m and 26n exhibited good inhibitory activities with Ki values of 0.39 and 0.33 μM, respectively. These low-molecular weight compounds are attractive leads for the further development of potent peptidomimetic inhibitors with pharmaceutical profiles. Docking studies were performed to model the binding interaction of the compound 26m with the SARS-CoV 3CL protease. The preliminary SAR study of the peptidomimetic compounds with potent inhibitory activities revealed several structural features that boosted the inhibitory activity: (i) a benzothiazole warhead at the S1' position, (ii) a γ-lactam unit at the S1-position, (iii) an appropriately hydrophobic leucine moiety at the S2-position, and (iv) a hydrogen bond between the N-arylglycine unit and a backbone hydrogen bond donor at the S3-position.

DOI: 10.1016/j.ejmech.2013.05.005
PubMed: 23747811

Affiliations:

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 001183
to stream PubMed, to step Curation: 001183

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pubmed:23747811

Le document en format XML

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<front><div type="abstract" xml:lang="en">This work describes the design, synthesis, and evaluation of low-molecular weight peptidic SARS-CoV 3CL protease inhibitors. The inhibitors were designed based on the potent tripeptidic Z-Val-Leu-Ala(pyrrolidone-3-yl)-2-benzothiazole (8; Ki = 4.1 nM), in which the P3 valine unit was substituted with a variety of distinct moieties. The resulting series of dipeptide-type inhibitors displayed moderate to good inhibitory activities against 3CL(pro). In particular, compounds 26m and 26n exhibited good inhibitory activities with Ki values of 0.39 and 0.33 μM, respectively. These low-molecular weight compounds are attractive leads for the further development of potent peptidomimetic inhibitors with pharmaceutical profiles. Docking studies were performed to model the binding interaction of the compound 26m with the SARS-CoV 3CL protease. The preliminary SAR study of the peptidomimetic compounds with potent inhibitory activities revealed several structural features that boosted the inhibitory activity: (i) a benzothiazole warhead at the S1' position, (ii) a γ-lactam unit at the S1-position, (iii) an appropriately hydrophobic leucine moiety at the S2-position, and (iv) a hydrogen bond between the N-arylglycine unit and a backbone hydrogen bond donor at the S3-position.</div>
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<Abstract><AbstractText>This work describes the design, synthesis, and evaluation of low-molecular weight peptidic SARS-CoV 3CL protease inhibitors. The inhibitors were designed based on the potent tripeptidic Z-Val-Leu-Ala(pyrrolidone-3-yl)-2-benzothiazole (8; Ki = 4.1 nM), in which the P3 valine unit was substituted with a variety of distinct moieties. The resulting series of dipeptide-type inhibitors displayed moderate to good inhibitory activities against 3CL(pro). In particular, compounds 26m and 26n exhibited good inhibitory activities with Ki values of 0.39 and 0.33 μM, respectively. These low-molecular weight compounds are attractive leads for the further development of potent peptidomimetic inhibitors with pharmaceutical profiles. Docking studies were performed to model the binding interaction of the compound 26m with the SARS-CoV 3CL protease. The preliminary SAR study of the peptidomimetic compounds with potent inhibitory activities revealed several structural features that boosted the inhibitory activity: (i) a benzothiazole warhead at the S1' position, (ii) a γ-lactam unit at the S1-position, (iii) an appropriately hydrophobic leucine moiety at the S2-position, and (iv) a hydrogen bond between the N-arylglycine unit and a backbone hydrogen bond donor at the S3-position.</AbstractText>
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Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: structure-activity relationship study.

Design, synthesis, and biological evaluation of novel dipeptide-type SARS-CoV 3CL protease inhibitors: structure-activity relationship study.

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