Echinomycin, a potential binder of FKBP12, shows minor effect on calcineurin activity.
Identifieur interne : 000E02 ( Main/Corpus ); précédent : 000E01; suivant : 000E03Echinomycin, a potential binder of FKBP12, shows minor effect on calcineurin activity.
Auteurs : Vikramjeet Singh ; Amita Nand ; Caixia Chen ; Zhipeng Li ; Sheng-Jie Li ; Songbai Wang ; Mo Yang ; Alejandro Merino ; Lixin Zhang ; Jingsong ZhuSource :
- Journal of biomolecular screening [ 1552-454X ] ; 2014.
English descriptors
- KwdEn :
- Calcineurin (chemistry), Calcineurin (metabolism), Echinomycin (chemistry), Echinomycin (metabolism), Echinomycin (pharmacology), Enzyme Activation (drug effects), Models, Biological (MeSH), Models, Molecular (MeSH), Molecular Conformation (MeSH), Molecular Docking Simulation (MeSH), Phosphoric Monoester Hydrolases (metabolism), Protein Binding (MeSH), Reproducibility of Results (MeSH), Signal Transduction (drug effects), Surface Plasmon Resonance (methods), Tacrolimus Binding Protein 1A (metabolism).
- MESH :
- chemical , chemistry : Calcineurin, Echinomycin.
- chemical , metabolism : Calcineurin, Echinomycin, Phosphoric Monoester Hydrolases, Tacrolimus Binding Protein 1A.
- chemical , pharmacology : Echinomycin.
- drug effects : Enzyme Activation, Signal Transduction.
- methods : Surface Plasmon Resonance.
- Models, Biological, Models, Molecular, Molecular Conformation, Molecular Docking Simulation, Protein Binding, Reproducibility of Results.
Abstract
Echinomycin, a member of the quinoxaline family of antibiotics, is known to be a small-molecule inhibitor of hypoxia inducible factor-1 (HIF-1) DNA binding activity. Recently, it has been shown to suppress mammalian target of rapamycin (mTOR) signaling and growth in leukemia cell lines. In this study, we investigated whether echinomycin interacts with the FKBP12 protein. Molecular docking was used, and the predicted binding energy was -10.61 kcal/mol. Moreover, surface plasmon resonance imaging and fluorescence quenching techniques were used to validate this interaction. Echinomycin binds to FKBP12 with a strong binding affinity comparable with rapamycin. Furthermore, the echinomycin-FKBP12 complex has been shown to affect calcineurin activity when tested in a calcineurin phosphatase inhibition assay. All of these studies have shown that echinomycin may have a double impact on HIF signaling by direct inhibition and through mTOR.
DOI: 10.1177/1087057114544742
PubMed: 25085862
Links to Exploration step
pubmed:25085862Le document en format XML
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Chen</name><affiliation><nlm:affiliation>Chinese Academy of Sciences Key Laboratory of Pathogenic Microbiology & Immunology, Institute of Microbiology, CAS, Beijing, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Li, Zhipeng" sort="Li, Zhipeng" uniqKey="Li Z" first="Zhipeng" last="Li">Zhipeng Li</name><affiliation><nlm:affiliation>College of Life Science and Bioengineering, Beijing University of Technology, Beijing, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Li, Sheng Jie" sort="Li, Sheng Jie" uniqKey="Li S" first="Sheng-Jie" last="Li">Sheng-Jie Li</name><affiliation><nlm:affiliation>Key Laboratory of Bioinformatics, School of Life Sciences, Tsinghua University, Beijing, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Wang, Songbai" sort="Wang, Songbai" uniqKey="Wang S" first="Songbai" last="Wang">Songbai Wang</name><affiliation><nlm:affiliation>National Center for Nanoscience and Technology, Beijing, People's Republic of China School of Chemistry and Chemical Engineering, Shanxi University, Taiyuan, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Mo" sort="Yang, Mo" uniqKey="Yang M" first="Mo" last="Yang">Mo Yang</name><affiliation><nlm:affiliation>National Center for Nanoscience and Technology, Beijing, People's Republic of China University of Chinese Academy of Sciences, Beijing, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Merino, Alejandro" sort="Merino, Alejandro" uniqKey="Merino A" first="Alejandro" last="Merino">Alejandro Merino</name><affiliation><nlm:affiliation>National Center for Nanoscience and Technology, Beijing, People's Republic of China University of Chinese Academy of Sciences, Beijing, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Zhang, Lixin" sort="Zhang, Lixin" uniqKey="Zhang L" first="Lixin" last="Zhang">Lixin Zhang</name><affiliation><nlm:affiliation>Chinese Academy of Sciences Key Laboratory of Pathogenic Microbiology & Immunology, Institute of Microbiology, CAS, Beijing, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Zhu, Jingsong" sort="Zhu, Jingsong" uniqKey="Zhu J" first="Jingsong" last="Zhu">Jingsong Zhu</name><affiliation><nlm:affiliation>National Center for Nanoscience and Technology, Beijing, People's Republic of China University of Chinese Academy of Sciences, Beijing, People's Republic of China jizhu@nanoctr.cn.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:25085862</idno><idno type="pmid">25085862</idno><idno type="doi">10.1177/1087057114544742</idno><idno type="wicri:Area/Main/Corpus">000E02</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000E02</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Echinomycin, a potential binder of FKBP12, shows minor effect on calcineurin activity.</title><author><name sortKey="Singh, Vikramjeet" sort="Singh, Vikramjeet" uniqKey="Singh V" first="Vikramjeet" last="Singh">Vikramjeet Singh</name><affiliation><nlm:affiliation>National Center for Nanoscience and Technology, Beijing, People's Republic of China University of Chinese Academy of Sciences, Beijing, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Nand, Amita" sort="Nand, Amita" uniqKey="Nand A" first="Amita" last="Nand">Amita Nand</name><affiliation><nlm:affiliation>National Center for Nanoscience and Technology, Beijing, People's Republic of China University of Chinese Academy of Sciences, Beijing, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Chen, Caixia" sort="Chen, Caixia" uniqKey="Chen C" first="Caixia" last="Chen">Caixia Chen</name><affiliation><nlm:affiliation>Chinese Academy of Sciences Key Laboratory of Pathogenic Microbiology & Immunology, Institute of Microbiology, CAS, Beijing, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Li, Zhipeng" sort="Li, Zhipeng" uniqKey="Li Z" first="Zhipeng" last="Li">Zhipeng Li</name><affiliation><nlm:affiliation>College of Life Science and Bioengineering, Beijing University of Technology, Beijing, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Li, Sheng Jie" sort="Li, Sheng Jie" uniqKey="Li S" first="Sheng-Jie" last="Li">Sheng-Jie Li</name><affiliation><nlm:affiliation>Key Laboratory of Bioinformatics, School of Life Sciences, Tsinghua University, Beijing, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Wang, Songbai" sort="Wang, Songbai" uniqKey="Wang S" first="Songbai" last="Wang">Songbai Wang</name><affiliation><nlm:affiliation>National Center for Nanoscience and Technology, Beijing, People's Republic of China School of Chemistry and Chemical Engineering, Shanxi University, Taiyuan, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Mo" sort="Yang, Mo" uniqKey="Yang M" first="Mo" last="Yang">Mo Yang</name><affiliation><nlm:affiliation>National Center for Nanoscience and Technology, Beijing, People's Republic of China University of Chinese Academy of Sciences, Beijing, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Merino, Alejandro" sort="Merino, Alejandro" uniqKey="Merino A" first="Alejandro" last="Merino">Alejandro Merino</name><affiliation><nlm:affiliation>National Center for Nanoscience and Technology, Beijing, People's Republic of China University of Chinese Academy of Sciences, Beijing, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Zhang, Lixin" sort="Zhang, Lixin" uniqKey="Zhang L" first="Lixin" last="Zhang">Lixin Zhang</name><affiliation><nlm:affiliation>Chinese Academy of Sciences Key Laboratory of Pathogenic Microbiology & Immunology, Institute of Microbiology, CAS, Beijing, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Zhu, Jingsong" sort="Zhu, Jingsong" uniqKey="Zhu J" first="Jingsong" last="Zhu">Jingsong Zhu</name><affiliation><nlm:affiliation>National Center for Nanoscience and Technology, Beijing, People's Republic of China University of Chinese Academy of Sciences, Beijing, People's Republic of China jizhu@nanoctr.cn.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Journal of biomolecular screening</title><idno type="eISSN">1552-454X</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Calcineurin (chemistry)</term><term>Calcineurin (metabolism)</term><term>Echinomycin (chemistry)</term><term>Echinomycin (metabolism)</term><term>Echinomycin (pharmacology)</term><term>Enzyme Activation (drug effects)</term><term>Models, Biological (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Conformation (MeSH)</term><term>Molecular Docking Simulation (MeSH)</term><term>Phosphoric Monoester Hydrolases (metabolism)</term><term>Protein Binding (MeSH)</term><term>Reproducibility of Results (MeSH)</term><term>Signal Transduction (drug effects)</term><term>Surface Plasmon Resonance (methods)</term><term>Tacrolimus Binding Protein 1A (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Calcineurin</term><term>Echinomycin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcineurin</term><term>Echinomycin</term><term>Phosphoric Monoester Hydrolases</term><term>Tacrolimus Binding Protein 1A</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Echinomycin</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Enzyme Activation</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Surface Plasmon Resonance</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Models, Biological</term><term>Models, Molecular</term><term>Molecular Conformation</term><term>Molecular Docking Simulation</term><term>Protein Binding</term><term>Reproducibility of Results</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Echinomycin, a member of the quinoxaline family of antibiotics, is known to be a small-molecule inhibitor of hypoxia inducible factor-1 (HIF-1) DNA binding activity. Recently, it has been shown to suppress mammalian target of rapamycin (mTOR) signaling and growth in leukemia cell lines. In this study, we investigated whether echinomycin interacts with the FKBP12 protein. Molecular docking was used, and the predicted binding energy was -10.61 kcal/mol. Moreover, surface plasmon resonance imaging and fluorescence quenching techniques were used to validate this interaction. Echinomycin binds to FKBP12 with a strong binding affinity comparable with rapamycin. Furthermore, the echinomycin-FKBP12 complex has been shown to affect calcineurin activity when tested in a calcineurin phosphatase inhibition assay. All of these studies have shown that echinomycin may have a double impact on HIF signaling by direct inhibition and through mTOR. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25085862</PMID><DateCompleted><Year>2015</Year><Month>06</Month><Day>10</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1552-454X</ISSN><JournalIssue CitedMedium="Internet"><Volume>19</Volume><Issue>9</Issue><PubDate><Year>2014</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Journal of biomolecular screening</Title><ISOAbbreviation>J Biomol Screen</ISOAbbreviation></Journal><ArticleTitle>Echinomycin, a potential binder of FKBP12, shows minor effect on calcineurin activity.</ArticleTitle><Pagination><MedlinePgn>1275-81</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1177/1087057114544742</ELocationID><Abstract><AbstractText>Echinomycin, a member of the quinoxaline family of antibiotics, is known to be a small-molecule inhibitor of hypoxia inducible factor-1 (HIF-1) DNA binding activity. Recently, it has been shown to suppress mammalian target of rapamycin (mTOR) signaling and growth in leukemia cell lines. In this study, we investigated whether echinomycin interacts with the FKBP12 protein. Molecular docking was used, and the predicted binding energy was -10.61 kcal/mol. Moreover, surface plasmon resonance imaging and fluorescence quenching techniques were used to validate this interaction. Echinomycin binds to FKBP12 with a strong binding affinity comparable with rapamycin. Furthermore, the echinomycin-FKBP12 complex has been shown to affect calcineurin activity when tested in a calcineurin phosphatase inhibition assay. All of these studies have shown that echinomycin may have a double impact on HIF signaling by direct inhibition and through mTOR. </AbstractText><CopyrightInformation>© 2014 Society for Laboratory Automation and Screening.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Singh</LastName><ForeName>Vikramjeet</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>National Center for Nanoscience and Technology, Beijing, People's Republic of China University of Chinese Academy of Sciences, Beijing, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nand</LastName><ForeName>Amita</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>National Center for Nanoscience and Technology, Beijing, People's Republic of China University of Chinese Academy of Sciences, Beijing, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Caixia</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Chinese Academy of Sciences Key Laboratory of Pathogenic Microbiology & Immunology, Institute of Microbiology, CAS, Beijing, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>ZhiPeng</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>College of Life Science and Bioengineering, Beijing University of Technology, Beijing, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Sheng-Jie</ForeName><Initials>SJ</Initials><AffiliationInfo><Affiliation>Key Laboratory of Bioinformatics, School of Life Sciences, Tsinghua University, Beijing, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Songbai</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>National Center for Nanoscience and Technology, Beijing, People's Republic of China School of Chemistry and Chemical Engineering, Shanxi University, Taiyuan, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Mo</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>National Center for Nanoscience and Technology, Beijing, People's Republic of China University of Chinese Academy of Sciences, Beijing, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Merino</LastName><ForeName>Alejandro</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>National Center for Nanoscience and Technology, Beijing, People's Republic of China University of Chinese Academy of Sciences, Beijing, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Lixin</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Chinese Academy of Sciences Key Laboratory of Pathogenic Microbiology & Immunology, Institute of Microbiology, CAS, Beijing, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhu</LastName><ForeName>Jingsong</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>National Center for Nanoscience and Technology, Beijing, People's Republic of China University of Chinese Academy of Sciences, Beijing, People's Republic of China jizhu@nanoctr.cn.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>08</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biomol Screen</MedlineTA><NlmUniqueID>9612112</NlmUniqueID><ISSNLinking>1087-0571</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>512-64-1</RegistryNumber><NameOfSubstance UI="D004448">Echinomycin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.-</RegistryNumber><NameOfSubstance UI="C120817">calcineurin phosphatase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.16</RegistryNumber><NameOfSubstance UI="D019703">Calcineurin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.2</RegistryNumber><NameOfSubstance UI="D010744">Phosphoric Monoester Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 5.2.1.-</RegistryNumber><NameOfSubstance UI="D022061">Tacrolimus Binding Protein 1A</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019703" MajorTopicYN="N">Calcineurin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004448" MajorTopicYN="N">Echinomycin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008968" MajorTopicYN="N">Molecular Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D062105" MajorTopicYN="N">Molecular Docking Simulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010744" MajorTopicYN="N">Phosphoric Monoester Hydrolases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015203" MajorTopicYN="N">Reproducibility of Results</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020349" MajorTopicYN="N">Surface Plasmon Resonance</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D022061" MajorTopicYN="N">Tacrolimus Binding Protein 1A</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">FK506-FKBP12-calcineurin</Keyword><Keyword MajorTopicYN="N">SPRi</Keyword><Keyword MajorTopicYN="N">echinomycin</Keyword><Keyword MajorTopicYN="N">fluorescence quenching</Keyword><Keyword MajorTopicYN="N">mTOR</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>8</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>8</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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