Virtual screening for finding natural inhibitor against cathepsin-L for SARS therapy.
Identifieur interne : 001C36 ( PubMed/Checkpoint ); précédent : 001C35; suivant : 001C37Virtual screening for finding natural inhibitor against cathepsin-L for SARS therapy.
Auteurs : S-Q Wang [République populaire de Chine] ; Q-S Du ; K. Zhao ; A-X Li ; D-Q Wei ; K-C ChouSource :
- Amino acids [ 1438-2199 ] ; 2007.
Descripteurs français
- KwdFr :
- Algorithmes, Bases de données factuelles, Cathepsine L, Cathepsines (antagonistes et inhibiteurs), Conformation moléculaire, Cysteine endopeptidases, Humains, Inhibiteurs de protéases (), Inhibiteurs de protéases (pharmacologie), Modèles moléculaires, Médicaments issus de plantes chinoises (), Médicaments issus de plantes chinoises (pharmacologie), Proenzymes (antagonistes et inhibiteurs), Préparations à base de plantes (), Préparations à base de plantes (pharmacologie), Simulation numérique, Structure moléculaire, Syndrome respiratoire aigu sévère (traitement médicamenteux), Évaluation préclinique de médicament.
- MESH :
- antagonistes et inhibiteurs : Cathepsines, Proenzymes.
- pharmacologie : Inhibiteurs de protéases, Médicaments issus de plantes chinoises, Préparations à base de plantes.
- traitement médicamenteux : Syndrome respiratoire aigu sévère.
- Algorithmes, Bases de données factuelles, Cathepsine L, Conformation moléculaire, Cysteine endopeptidases, Humains, Inhibiteurs de protéases, Modèles moléculaires, Médicaments issus de plantes chinoises, Préparations à base de plantes, Simulation numérique, Structure moléculaire, Évaluation préclinique de médicament.
English descriptors
- KwdEn :
- Algorithms, Cathepsin L, Cathepsins (antagonists & inhibitors), Computer Simulation, Cysteine Endopeptidases, Databases, Factual, Drug Evaluation, Preclinical, Drugs, Chinese Herbal (chemistry), Drugs, Chinese Herbal (pharmacology), Enzyme Precursors (antagonists & inhibitors), Humans, Models, Molecular, Molecular Conformation, Molecular Structure, Plant Preparations (chemistry), Plant Preparations (pharmacology), Protease Inhibitors (chemistry), Protease Inhibitors (pharmacology), Severe Acute Respiratory Syndrome (drug therapy).
- MESH :
- chemical , antagonists & inhibitors : Cathepsins, Enzyme Precursors.
- chemical , chemistry : Drugs, Chinese Herbal, Plant Preparations, Protease Inhibitors.
- chemical , pharmacology : Drugs, Chinese Herbal, Plant Preparations, Protease Inhibitors.
- chemical : Cathepsin L, Cysteine Endopeptidases.
- drug therapy : Severe Acute Respiratory Syndrome.
- Algorithms, Computer Simulation, Databases, Factual, Drug Evaluation, Preclinical, Humans, Models, Molecular, Molecular Conformation, Molecular Structure.
Abstract
Recently Simmons et al. reported a new mechanism for SARS virus entry into target cells, where MDL28170 was identified as an efficient inhibitor of CTSL-meditated substrate cleavage with IC(50) of 2.5 nmol/l. Based on the molecule fingerprint searching method, 11 natural molecules were found in the Traditional Chinese Medicines Database (TCMD). Molecular simulation indicates that the MOL376 (a compound derived from a Chinese medicine herb with the therapeutic efficacy on the human body such as relieving cough, removing the phlegm, and relieving asthma) has not only the highest binding energy with the receptor but also the good match in geometric conformation. It was observed through docking studies that the van der Waals interactions made substantial contributions to the affinity, and that the receptor active pocket was too large for MDL21870 but more suitable for MOL736. Accordingly, MOL736 might possibly become a promising lead compound for CTSL inhibition for SARS therapy.
DOI: 10.1007/s00726-006-0403-1
PubMed: 16998715
Affiliations:
Links toward previous steps (curation, corpus...)
Links to Exploration step
pubmed:16998715Le document en format XML
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<term>Syndrome respiratoire aigu sévère (traitement médicamenteux)</term>
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<term>Cysteine endopeptidases</term>
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<front><div type="abstract" xml:lang="en">Recently Simmons et al. reported a new mechanism for SARS virus entry into target cells, where MDL28170 was identified as an efficient inhibitor of CTSL-meditated substrate cleavage with IC(50) of 2.5 nmol/l. Based on the molecule fingerprint searching method, 11 natural molecules were found in the Traditional Chinese Medicines Database (TCMD). Molecular simulation indicates that the MOL376 (a compound derived from a Chinese medicine herb with the therapeutic efficacy on the human body such as relieving cough, removing the phlegm, and relieving asthma) has not only the highest binding energy with the receptor but also the good match in geometric conformation. It was observed through docking studies that the van der Waals interactions made substantial contributions to the affinity, and that the receptor active pocket was too large for MDL21870 but more suitable for MOL736. Accordingly, MOL736 might possibly become a promising lead compound for CTSL inhibition for SARS therapy.</div>
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<Abstract><AbstractText>Recently Simmons et al. reported a new mechanism for SARS virus entry into target cells, where MDL28170 was identified as an efficient inhibitor of CTSL-meditated substrate cleavage with IC(50) of 2.5 nmol/l. Based on the molecule fingerprint searching method, 11 natural molecules were found in the Traditional Chinese Medicines Database (TCMD). Molecular simulation indicates that the MOL376 (a compound derived from a Chinese medicine herb with the therapeutic efficacy on the human body such as relieving cough, removing the phlegm, and relieving asthma) has not only the highest binding energy with the receptor but also the good match in geometric conformation. It was observed through docking studies that the van der Waals interactions made substantial contributions to the affinity, and that the receptor active pocket was too large for MDL21870 but more suitable for MOL736. Accordingly, MOL736 might possibly become a promising lead compound for CTSL inhibition for SARS therapy.</AbstractText>
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<affiliations><list><country><li>République populaire de Chine</li>
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