The interaction between severe acute respiratory syndrome coronavirus 3C-like proteinase and a dimeric inhibitor by capillary electrophoresis.
Identifieur interne : 000F87 ( Ncbi/Merge ); précédent : 000F86; suivant : 000F88The interaction between severe acute respiratory syndrome coronavirus 3C-like proteinase and a dimeric inhibitor by capillary electrophoresis.
Auteurs : Li Ding [République populaire de Chine] ; Xin-Xiang Zhang ; Ping Wei ; Keqiang Fan ; Luhua LaiSource :
- Analytical biochemistry [ 0003-2697 ] ; 2005.
Descripteurs français
- KwdFr :
- Cysteine endopeptidases (), Cysteine endopeptidases (métabolisme), Dimérisation, Inhibiteurs de protéases (), Inhibiteurs de protéases (métabolisme), Liaison aux protéines, Oligopeptides (), Oligopeptides (métabolisme), Protéines virales (), Protéines virales (antagonistes et inhibiteurs), Protéines virales (métabolisme), Virus du SRAS (enzymologie), Électrophorèse capillaire (), Évaluation préclinique de médicament ().
- MESH :
- antagonistes et inhibiteurs : Protéines virales.
- enzymologie : Virus du SRAS.
- métabolisme : Cysteine endopeptidases, Inhibiteurs de protéases, Oligopeptides, Protéines virales.
- Cysteine endopeptidases, Dimérisation, Inhibiteurs de protéases, Liaison aux protéines, Oligopeptides, Protéines virales, Électrophorèse capillaire, Évaluation préclinique de médicament.
English descriptors
- KwdEn :
- Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (metabolism), Dimerization, Drug Evaluation, Preclinical (methods), Electrophoresis, Capillary (methods), Oligopeptides (chemistry), Oligopeptides (metabolism), Protease Inhibitors (chemistry), Protease Inhibitors (metabolism), Protein Binding, SARS Virus (enzymology), Viral Proteins (antagonists & inhibitors), Viral Proteins (chemistry), Viral Proteins (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Viral Proteins.
- chemical , chemistry : Cysteine Endopeptidases, Oligopeptides, Protease Inhibitors, Viral Proteins.
- chemical , metabolism : Cysteine Endopeptidases, Oligopeptides, Protease Inhibitors, Viral Proteins.
- enzymology : SARS Virus.
- methods : Drug Evaluation, Preclinical, Electrophoresis, Capillary.
- Dimerization, Protein Binding.
Abstract
3C-like proteinase of severe acute respiratory syndrome (SARS) coronavirus has been demonstrated to be a key target for drug design against SARS. The interaction between SARS coronavirus 3C-like (3CL) proteinase and an octapeptide interface inhibitor was studied by affinity capillary electrophoresis (ACE). The binding constants were estimated by the change of migration time of the analytes in the buffer solution containing different concentrations of SARS 3CL proteinase. The results showed that SARS 3CL proteinase was able to complex with the octapeptide competitively, with binding constants of 2.44 x 10(4) M(-1) at 20 degrees C and 2.11 x 10(4)M(-1) at 37 degrees C. In addition, the thermodynamic parameters deduced reveal that hydrophobic interaction might play major roles, along with electrostatic force, in the binding process. The ACE method used here could be developed to be an effective and simple way of applying large-scale drug screening and evaluation.
DOI: 10.1016/j.ab.2005.04.027
PubMed: 15935325
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last="Zhang">Xin-Xiang Zhang</name></author><author><name sortKey="Wei, Ping" sort="Wei, Ping" uniqKey="Wei P" first="Ping" last="Wei">Ping Wei</name></author><author><name sortKey="Fan, Keqiang" sort="Fan, Keqiang" uniqKey="Fan K" first="Keqiang" last="Fan">Keqiang Fan</name></author><author><name sortKey="Lai, Luhua" sort="Lai, Luhua" uniqKey="Lai L" first="Luhua" last="Lai">Luhua Lai</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:15935325</idno><idno type="pmid">15935325</idno><idno type="doi">10.1016/j.ab.2005.04.027</idno><idno type="wicri:Area/PubMed/Corpus">002703</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002703</idno><idno type="wicri:Area/PubMed/Curation">002703</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002703</idno><idno type="wicri:Area/PubMed/Checkpoint">002431</idno><idno 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Preclinical (methods)</term><term>Electrophoresis, Capillary (methods)</term><term>Oligopeptides (chemistry)</term><term>Oligopeptides (metabolism)</term><term>Protease Inhibitors (chemistry)</term><term>Protease Inhibitors (metabolism)</term><term>Protein Binding</term><term>SARS Virus (enzymology)</term><term>Viral Proteins (antagonists & inhibitors)</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cysteine endopeptidases ()</term><term>Cysteine endopeptidases (métabolisme)</term><term>Dimérisation</term><term>Inhibiteurs de protéases ()</term><term>Inhibiteurs de protéases (métabolisme)</term><term>Liaison aux protéines</term><term>Oligopeptides ()</term><term>Oligopeptides (métabolisme)</term><term>Protéines virales ()</term><term>Protéines virales (antagonistes et inhibiteurs)</term><term>Protéines virales (métabolisme)</term><term>Virus du SRAS (enzymologie)</term><term>Électrophorèse capillaire ()</term><term>Évaluation préclinique de médicament ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Oligopeptides</term><term>Protease Inhibitors</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Oligopeptides</term><term>Protease Inhibitors</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Protéines virales</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Drug Evaluation, Preclinical</term><term>Electrophoresis, Capillary</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cysteine endopeptidases</term><term>Inhibiteurs de protéases</term><term>Oligopeptides</term><term>Protéines virales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Dimerization</term><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cysteine endopeptidases</term><term>Dimérisation</term><term>Inhibiteurs de protéases</term><term>Liaison aux protéines</term><term>Oligopeptides</term><term>Protéines virales</term><term>Électrophorèse capillaire</term><term>Évaluation préclinique de médicament</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">3C-like proteinase of severe acute respiratory syndrome (SARS) coronavirus has been demonstrated to be a key target for drug design against SARS. The interaction between SARS coronavirus 3C-like (3CL) proteinase and an octapeptide interface inhibitor was studied by affinity capillary electrophoresis (ACE). The binding constants were estimated by the change of migration time of the analytes in the buffer solution containing different concentrations of SARS 3CL proteinase. The results showed that SARS 3CL proteinase was able to complex with the octapeptide competitively, with binding constants of 2.44 x 10(4) M(-1) at 20 degrees C and 2.11 x 10(4)M(-1) at 37 degrees C. In addition, the thermodynamic parameters deduced reveal that hydrophobic interaction might play major roles, along with electrostatic force, in the binding process. The ACE method used here could be developed to be an effective and simple way of applying large-scale drug screening and evaluation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15935325</PMID><DateCompleted><Year>2005</Year><Month>10</Month><Day>17</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-2697</ISSN><JournalIssue CitedMedium="Print"><Volume>343</Volume><Issue>1</Issue><PubDate><Year>2005</Year><Month>Aug</Month><Day>01</Day></PubDate></JournalIssue><Title>Analytical biochemistry</Title><ISOAbbreviation>Anal. Biochem.</ISOAbbreviation></Journal><ArticleTitle>The interaction between severe acute respiratory syndrome coronavirus 3C-like proteinase and a dimeric inhibitor by capillary electrophoresis.</ArticleTitle><Pagination><MedlinePgn>159-65</MedlinePgn></Pagination><Abstract><AbstractText>3C-like proteinase of severe acute respiratory syndrome (SARS) coronavirus has been demonstrated to be a key target for drug design against SARS. The interaction between SARS coronavirus 3C-like (3CL) proteinase and an octapeptide interface inhibitor was studied by affinity capillary electrophoresis (ACE). The binding constants were estimated by the change of migration time of the analytes in the buffer solution containing different concentrations of SARS 3CL proteinase. The results showed that SARS 3CL proteinase was able to complex with the octapeptide competitively, with binding constants of 2.44 x 10(4) M(-1) at 20 degrees C and 2.11 x 10(4)M(-1) at 37 degrees C. In addition, the thermodynamic parameters deduced reveal that hydrophobic interaction might play major roles, along with electrostatic force, in the binding process. The ACE method used here could be developed to be an effective and simple way of applying large-scale drug screening and evaluation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ding</LastName><ForeName>Li</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Xin-Xiang</ForeName><Initials>XX</Initials></Author><Author ValidYN="Y"><LastName>Wei</LastName><ForeName>Ping</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Fan</LastName><ForeName>Keqiang</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Lai</LastName><ForeName>Luhua</ForeName><Initials>L</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType 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