Reducing agents affect inhibitory activities of compounds: results from multiple drug targets.
Identifieur interne : 001410 ( PubMed/Corpus ); précédent : 001409; suivant : 001411Reducing agents affect inhibitory activities of compounds: results from multiple drug targets.
Auteurs : Hyun Lee ; Jaime Torres ; Lena Truong ; Rima Chaudhuri ; Anuradha Mittal ; Michael E. JohnsonSource :
- Analytical biochemistry [ 1096-0309 ] ; 2012.
English descriptors
- KwdEn :
- Dithiothreitol (chemistry), Glutathione (chemistry), Hepacivirus (enzymology), High-Throughput Screening Assays, Kinetics, Mercaptoethanol (chemistry), Peptide Hydrolases (chemistry), Peptide Hydrolases (metabolism), Phosphines (chemistry), Protease Inhibitors (chemistry), Proteins (antagonists & inhibitors), Proteins (metabolism), SARS Virus (enzymology), Viral Nonstructural Proteins (antagonists & inhibitors), Viral Nonstructural Proteins (metabolism), Viral Proteins (antagonists & inhibitors), Viral Proteins (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Proteins, Viral Nonstructural Proteins, Viral Proteins.
- chemical , chemistry : Dithiothreitol, Glutathione, Mercaptoethanol, Peptide Hydrolases, Phosphines, Protease Inhibitors.
- enzymology : Hepacivirus, SARS Virus.
- chemical , metabolism : Peptide Hydrolases, Proteins, Viral Nonstructural Proteins, Viral Proteins.
- High-Throughput Screening Assays, Kinetics.
Abstract
High-throughput screening (HTS) of large compound libraries has become a commonly used method for the identification of drug leads, and nonphysiological reducing agents have been widely used for HTS. However, a comparison of the difference in the HTS results based on the choice of reducing agent used and potency comparisons of selected inhibitors has not been done with the physiological reducing agent reduced glutathione (GSH). Here, we compared the effects of three reducing agents-dithiothreitol (DTT), β-mercaptoethanol (β-MCE), and tris(2-carboxyethyl)phosphine (TCEP)-as well as GSH against three drug target proteins. Approximately 100,000 compounds were computationally screened for each target protein, and experimental testing of high-scoring compounds (~560 compounds) with the four reducing agents surprisingly produced many nonoverlapping hits. More importantly, we found that various reducing agents altered inhibitor potency (IC(50)) from approximately 10 μM with one reducing agent to complete loss (IC(50)>200 μM) of inhibitory activity with another reducing agent. Therefore, the choice of reducing agent in an HTS is critical because this may lead to the pursuit of falsely identified active compounds or failure to identify the true active compounds. We demonstrate the feasibility of using GSH for in vitro HTS assays with these three target enzymes.
DOI: 10.1016/j.ab.2012.01.006
PubMed: 22310499
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pubmed:22310499Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Reducing agents affect inhibitory activities of compounds: results from multiple drug targets.</title><author><name sortKey="Lee, Hyun" sort="Lee, Hyun" uniqKey="Lee H" first="Hyun" last="Lee">Hyun Lee</name><affiliation><nlm:affiliation>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, Chicago, IL 60607, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Torres, Jaime" sort="Torres, Jaime" uniqKey="Torres J" first="Jaime" last="Torres">Jaime Torres</name></author><author><name sortKey="Truong, Lena" sort="Truong, Lena" uniqKey="Truong L" first="Lena" last="Truong">Lena Truong</name></author><author><name sortKey="Chaudhuri, Rima" sort="Chaudhuri, Rima" uniqKey="Chaudhuri R" first="Rima" last="Chaudhuri">Rima Chaudhuri</name></author><author><name sortKey="Mittal, Anuradha" sort="Mittal, Anuradha" uniqKey="Mittal A" first="Anuradha" last="Mittal">Anuradha Mittal</name></author><author><name sortKey="Johnson, Michael E" sort="Johnson, Michael E" uniqKey="Johnson M" first="Michael E" last="Johnson">Michael E. Johnson</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:22310499</idno><idno type="pmid">22310499</idno><idno type="doi">10.1016/j.ab.2012.01.006</idno><idno type="wicri:Area/PubMed/Corpus">001410</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001410</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Reducing agents affect inhibitory activities of compounds: results from multiple drug targets.</title><author><name sortKey="Lee, Hyun" sort="Lee, Hyun" uniqKey="Lee H" first="Hyun" last="Lee">Hyun Lee</name><affiliation><nlm:affiliation>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, Chicago, IL 60607, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Torres, Jaime" sort="Torres, Jaime" uniqKey="Torres J" first="Jaime" last="Torres">Jaime Torres</name></author><author><name sortKey="Truong, Lena" sort="Truong, Lena" uniqKey="Truong L" first="Lena" last="Truong">Lena Truong</name></author><author><name sortKey="Chaudhuri, Rima" sort="Chaudhuri, Rima" uniqKey="Chaudhuri R" first="Rima" last="Chaudhuri">Rima Chaudhuri</name></author><author><name sortKey="Mittal, Anuradha" sort="Mittal, Anuradha" uniqKey="Mittal A" first="Anuradha" last="Mittal">Anuradha Mittal</name></author><author><name sortKey="Johnson, Michael E" sort="Johnson, Michael E" uniqKey="Johnson M" first="Michael E" last="Johnson">Michael E. Johnson</name></author></analytic><series><title level="j">Analytical biochemistry</title><idno type="eISSN">1096-0309</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Dithiothreitol (chemistry)</term><term>Glutathione (chemistry)</term><term>Hepacivirus (enzymology)</term><term>High-Throughput Screening Assays</term><term>Kinetics</term><term>Mercaptoethanol (chemistry)</term><term>Peptide Hydrolases (chemistry)</term><term>Peptide Hydrolases (metabolism)</term><term>Phosphines (chemistry)</term><term>Protease Inhibitors (chemistry)</term><term>Proteins (antagonists & inhibitors)</term><term>Proteins (metabolism)</term><term>SARS Virus (enzymology)</term><term>Viral Nonstructural Proteins (antagonists & inhibitors)</term><term>Viral Nonstructural Proteins (metabolism)</term><term>Viral Proteins (antagonists & inhibitors)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Proteins</term><term>Viral Nonstructural Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Dithiothreitol</term><term>Glutathione</term><term>Mercaptoethanol</term><term>Peptide Hydrolases</term><term>Phosphines</term><term>Protease Inhibitors</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Hepacivirus</term><term>SARS Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptide Hydrolases</term><term>Proteins</term><term>Viral Nonstructural Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>High-Throughput Screening Assays</term><term>Kinetics</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">High-throughput screening (HTS) of large compound libraries has become a commonly used method for the identification of drug leads, and nonphysiological reducing agents have been widely used for HTS. However, a comparison of the difference in the HTS results based on the choice of reducing agent used and potency comparisons of selected inhibitors has not been done with the physiological reducing agent reduced glutathione (GSH). Here, we compared the effects of three reducing agents-dithiothreitol (DTT), β-mercaptoethanol (β-MCE), and tris(2-carboxyethyl)phosphine (TCEP)-as well as GSH against three drug target proteins. Approximately 100,000 compounds were computationally screened for each target protein, and experimental testing of high-scoring compounds (~560 compounds) with the four reducing agents surprisingly produced many nonoverlapping hits. More importantly, we found that various reducing agents altered inhibitor potency (IC(50)) from approximately 10 μM with one reducing agent to complete loss (IC(50)>200 μM) of inhibitory activity with another reducing agent. Therefore, the choice of reducing agent in an HTS is critical because this may lead to the pursuit of falsely identified active compounds or failure to identify the true active compounds. We demonstrate the feasibility of using GSH for in vitro HTS assays with these three target enzymes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22310499</PMID><DateCompleted><Year>2012</Year><Month>07</Month><Day>09</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1096-0309</ISSN><JournalIssue CitedMedium="Internet"><Volume>423</Volume><Issue>1</Issue><PubDate><Year>2012</Year><Month>Apr</Month><Day>01</Day></PubDate></JournalIssue><Title>Analytical biochemistry</Title><ISOAbbreviation>Anal. Biochem.</ISOAbbreviation></Journal><ArticleTitle>Reducing agents affect inhibitory activities of compounds: results from multiple drug targets.</ArticleTitle><Pagination><MedlinePgn>46-53</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ab.2012.01.006</ELocationID><Abstract><AbstractText>High-throughput screening (HTS) of large compound libraries has become a commonly used method for the identification of drug leads, and nonphysiological reducing agents have been widely used for HTS. However, a comparison of the difference in the HTS results based on the choice of reducing agent used and potency comparisons of selected inhibitors has not been done with the physiological reducing agent reduced glutathione (GSH). Here, we compared the effects of three reducing agents-dithiothreitol (DTT), β-mercaptoethanol (β-MCE), and tris(2-carboxyethyl)phosphine (TCEP)-as well as GSH against three drug target proteins. Approximately 100,000 compounds were computationally screened for each target protein, and experimental testing of high-scoring compounds (~560 compounds) with the four reducing agents surprisingly produced many nonoverlapping hits. More importantly, we found that various reducing agents altered inhibitor potency (IC(50)) from approximately 10 μM with one reducing agent to complete loss (IC(50)>200 μM) of inhibitory activity with another reducing agent. Therefore, the choice of reducing agent in an HTS is critical because this may lead to the pursuit of falsely identified active compounds or failure to identify the true active compounds. We demonstrate the feasibility of using GSH for in vitro HTS assays with these three target enzymes.</AbstractText><CopyrightInformation>Copyright © 2012 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Hyun</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, Chicago, IL 60607, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Torres</LastName><ForeName>Jaime</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Truong</LastName><ForeName>Lena</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Chaudhuri</LastName><ForeName>Rima</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Mittal</LastName><ForeName>Anuradha</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Johnson</LastName><ForeName>Michael E</ForeName><Initials>ME</Initials></Author></AuthorList><Language>eng</Language><GrantList 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