About: The interaction between severe acute respiratory syndrome coronavirus 3C-like proteinase and a dimeric inhibitor by capillary electrophoresis

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About: The interaction between severe acute respiratory syndrome coronavirus 3C-like proteinase and a dimeric inhibitor by capillary electrophoresis Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The interaction between severe acute respiratory syndrome coronavirus 3C-like proteinase and a dimeric inhibitor by capillary electrophoresis
Creator	Ding, Li Wei, Ping Fan, Keqiang Lai, Luhua Zhang, Xin-Xiang
Source	Elsevier; Medline; PMC
abstract	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 2.44×104 M−1 at 20°C and 2.11×104 M−1 at 37°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.
has issue date	2005-08-01(xsd:dateTime)
bibo:doi	10.1016/j.ab.2005.04.027
bibo:pmid	15935325
has license	els-covid
sha1sum (hex)	78bf9490c6db6b9cda7984151b16b6415e1c0ce9
schema:url	https://doi.org/10.1016/j.ab.2005.04.027
resource representing a document's title	The interaction between severe acute respiratory syndrome coronavirus 3C-like proteinase and a dimeric inhibitor by capillary electrophoresis
has PubMed Central identifier	PMC7094366
has PubMed identifier	15935325
schema:publication	Analytical Biochemistry
resource representing a document's body	covid:78bf9490c6db6b9cda7984151b16b6415e1c0ce9#body_text
is schema:about of	named entity 'LIKE' named entity 'studied' named entity 'demonstrated' named entity 'proteinase' named entity 'USED' named entity 'MAJOR' named entity 'INHIBITOR' named entity 'DEMONSTRATED' named entity 'HYDROPHOBIC INTERACTION' named entity 'THE CHANGE' named entity 'INTERACTION' named entity 'AFFINITY' named entity 'DRUG SCREENING' named entity 'BINDING' named entity 'FORCE' named entity 'CAPILLARY ELECTROPHORESIS' named entity 'CORONAVIRUS' named entity 'CONTAINING' named entity 'EFFECTIVE' named entity 'TARGET' named entity 'REVEAL' named entity 'ELECTROSTATIC' named entity 'SARS CORONAVIRUS' named entity 'LARGE' named entity 'EVALUATION' named entity 'MIGRATION' named entity 'DIFFERENT' named entity 'PARAMETERS' named entity '20%' named entity 'PROTEINASE' named entity 'INTERACTION' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS' covid:arg/78bf9490c6db6b9cda7984151b16b6415e1c0ce9 named entity 'WAY' named entity 'PLAY' named entity 'SIMPLE' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME' named entity 'ESTIMATED' named entity 'ACE' named entity 'DRUG DESIGN' named entity 'ANALYTES' named entity 'METHOD' named entity 'RESULTS' named entity 'PROTEINASE' named entity 'APPLYING' named entity 'COMPLEX' named entity 'KEY' named entity 'INHIBITOR' named entity 'BUFFER SOLUTION' named entity 'TIME' named entity 'HERE' named entity 'ROLES' named entity 'CAPILLARY ELECTROPHORESIS' named entity 'INTERFACE' named entity 'COULD BE' named entity 'SARS' named entity 'CONSTANTS' named entity 'PROCESS' named entity 'THERMODYNAMIC' named entity 'ADDITION' named entity 'LIKE' named entity 'SCALE' named entity 'CONCENTRATIONS' named entity 'constants' named entity 'analytes' named entity 'process' named entity 'developed' named entity 'affinity capillary electrophoresis' named entity 'addition' named entity 'inhibitor' named entity 'proteinase' named entity 'proteinase' named entity 'buffer solution' named entity 'affinity capillary electrophoresis' named entity 'octapeptide' named entity 'thermodynamic' named entity 'electrostatic force'

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