Development of diaminoquinazoline histone lysine methyltransferase inhibitors as potent blood-stage antimalarial compounds.
Identifieur interne : 003286 ( PubMed/Curation ); précédent : 003285; suivant : 003287Development of diaminoquinazoline histone lysine methyltransferase inhibitors as potent blood-stage antimalarial compounds.
Auteurs : Sandeep Sundriyal [Royaume-Uni] ; Nicholas A. Malmquist [France] ; Joachim Caron [Royaume-Uni] ; Scott Blundell [Australie] ; Feng Liu [États-Unis] ; Xin Chen [États-Unis] ; Nitipol Srimongkolpithak [Royaume-Uni] ; Jian Jin [États-Unis] ; Susan A. Charman [Australie] ; Artur Scherf [France] ; Matthew J. Fuchter [Royaume-Uni]Source :
- ChemMedChem [ 1860-7187 ] ; 2014.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Plasmodium falciparum.
- métabolisme : Histone-lysine N-methyltransferase.
- pharmacologie : Antipaludiques, Quinazolines.
- Animaux, Plasmodium falciparum.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Histone-Lysine N-Methyltransferase.
- chemical , pharmacology : Antimalarials, Quinazolines.
- drug effects : Plasmodium falciparum.
- enzymology : Plasmodium falciparum.
- Animals.
Abstract
Modulating epigenetic mechanisms in malarial parasites is an emerging avenue for the discovery of novel antimalarial drugs. Previously we demonstrated the potent in vitro and in vivo antimalarial activity of (1-benzyl-4-piperidyl)[6,7-dimethoxy-2-(4-methyl-1,4-diazepin-1-yl)-4-quinazolinyl]amine (BIX01294; 1), a known human G9a inhibitor, together with its dose-dependent effects on histone methylation in the malarial parasite. This work describes our initial medicinal chemistry efforts to optimise the diaminoquinazoline chemotype for antimalarial activity. A variety of analogues were designed by substituting the 2 and 4 positions of the quinazoline core, and these molecules were tested against Plasmodium falciparum (3D7 strain). Several analogues with IC50 values as low as 18.5 nM and with low mammalian cell toxicity (HepG2) were identified. Certain pharmacophoric features required for antimalarial activity were found to be analogous to the previously published SAR of these analogues for G9a inhibition, thereby suggesting potential similarities between the malarial and human HKMT targets of this chemotype. Physiochemical, in vitro activity, and in vitro metabolism studies were also performed for a select set of potent analogues to evaluate their potential as antimalarial leads.
DOI: 10.1002/cmdc.201402098
PubMed: 25044750
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Charman</name><affiliation wicri:level="1"><nlm:affiliation>Monash Institute of Pharmaceutical Sciences, 381 Royal Parade, Parkville, Victoria 3052, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Monash Institute of Pharmaceutical Sciences, 381 Royal Parade, Parkville, Victoria 3052</wicri:regionArea></affiliation></author><author><name sortKey="Scherf, Artur" sort="Scherf, Artur" uniqKey="Scherf A" first="Artur" last="Scherf">Artur Scherf</name><affiliation wicri:level="1"><nlm:affiliation>Unité de Biologie des Interactions Hôte-Parasite, Institut Pasteur, F-75724 Paris CEDEX 15, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Unité de Biologie des Interactions Hôte-Parasite, Institut Pasteur, F-75724 Paris CEDEX 15</wicri:regionArea></affiliation></author><author><name sortKey="Fuchter, Matthew J" sort="Fuchter, Matthew J" uniqKey="Fuchter M" first="Matthew J" last="Fuchter">Matthew J. Fuchter</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, Imperial College London, London SW7 2AZ, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Chemistry, Imperial College London, London SW7 2AZ</wicri:regionArea></affiliation></author></analytic><series><title level="j">ChemMedChem</title><idno type="eISSN">1860-7187</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antimalarials (pharmacology)</term><term>Histone-Lysine N-Methyltransferase (metabolism)</term><term>Plasmodium falciparum (drug effects)</term><term>Plasmodium falciparum (enzymology)</term><term>Quinazolines (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Antipaludiques (pharmacologie)</term><term>Histone-lysine N-methyltransferase (métabolisme)</term><term>Plasmodium falciparum ()</term><term>Plasmodium falciparum (enzymologie)</term><term>Quinazolines (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Histone-Lysine N-Methyltransferase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antimalarials</term><term>Quinazolines</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Plasmodium falciparum</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Plasmodium falciparum</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Plasmodium falciparum</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Histone-lysine N-methyltransferase</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antipaludiques</term><term>Quinazolines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Plasmodium falciparum</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Modulating epigenetic mechanisms in malarial parasites is an emerging avenue for the discovery of novel antimalarial drugs. Previously we demonstrated the potent in vitro and in vivo antimalarial activity of (1-benzyl-4-piperidyl)[6,7-dimethoxy-2-(4-methyl-1,4-diazepin-1-yl)-4-quinazolinyl]amine (BIX01294; 1), a known human G9a inhibitor, together with its dose-dependent effects on histone methylation in the malarial parasite. This work describes our initial medicinal chemistry efforts to optimise the diaminoquinazoline chemotype for antimalarial activity. A variety of analogues were designed by substituting the 2 and 4 positions of the quinazoline core, and these molecules were tested against Plasmodium falciparum (3D7 strain). Several analogues with IC50 values as low as 18.5 nM and with low mammalian cell toxicity (HepG2) were identified. Certain pharmacophoric features required for antimalarial activity were found to be analogous to the previously published SAR of these analogues for G9a inhibition, thereby suggesting potential similarities between the malarial and human HKMT targets of this chemotype. Physiochemical, in vitro activity, and in vitro metabolism studies were also performed for a select set of potent analogues to evaluate their potential as antimalarial leads.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25044750</PMID><DateCreated><Year>2014</Year><Month>09</Month><Day>26</Day></DateCreated><DateCompleted><Year>2015</Year><Month>05</Month><Day>20</Day></DateCompleted><DateRevised><Year>2017</Year><Month>07</Month><Day>18</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1860-7187</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>10</Issue><PubDate><Year>2014</Year><Month>Oct</Month></PubDate></JournalIssue><Title>ChemMedChem</Title><ISOAbbreviation>ChemMedChem</ISOAbbreviation></Journal><ArticleTitle>Development of diaminoquinazoline histone lysine methyltransferase inhibitors as potent blood-stage antimalarial compounds.</ArticleTitle><Pagination><MedlinePgn>2360-2373</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/cmdc.201402098</ELocationID><Abstract><AbstractText>Modulating epigenetic mechanisms in malarial parasites is an emerging avenue for the discovery of novel antimalarial drugs. Previously we demonstrated the potent in vitro and in vivo antimalarial activity of (1-benzyl-4-piperidyl)[6,7-dimethoxy-2-(4-methyl-1,4-diazepin-1-yl)-4-quinazolinyl]amine (BIX01294; 1), a known human G9a inhibitor, together with its dose-dependent effects on histone methylation in the malarial parasite. This work describes our initial medicinal chemistry efforts to optimise the diaminoquinazoline chemotype for antimalarial activity. A variety of analogues were designed by substituting the 2 and 4 positions of the quinazoline core, and these molecules were tested against Plasmodium falciparum (3D7 strain). Several analogues with IC50 values as low as 18.5 nM and with low mammalian cell toxicity (HepG2) were identified. Certain pharmacophoric features required for antimalarial activity were found to be analogous to the previously published SAR of these analogues for G9a inhibition, thereby suggesting potential similarities between the malarial and human HKMT targets of this chemotype. Physiochemical, in vitro activity, and in vitro metabolism studies were also performed for a select set of potent analogues to evaluate their potential as antimalarial leads.</AbstractText><CopyrightInformation>© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y" EqualContrib="Y"><LastName>Sundriyal</LastName><ForeName>Sandeep</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Imperial College London, London SW7 2AZ, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y" EqualContrib="Y"><LastName>Malmquist</LastName><ForeName>Nicholas A</ForeName><Initials>NA</Initials><AffiliationInfo><Affiliation>Unité de Biologie des Interactions Hôte-Parasite, Institut Pasteur, F-75724 Paris CEDEX 15, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Centre National de la Recherche Scientifique, Unité de Recherche Associée 2581, F-75724 Paris CEDEX 15, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Caron</LastName><ForeName>Joachim</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Imperial College London, London SW7 2AZ, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Blundell</LastName><ForeName>Scott</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Monash Institute of Pharmaceutical Sciences, 381 Royal Parade, Parkville, Victoria 3052, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Feng</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Center for Integrative Chemical Biology and Drug Discovery, Division of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, 26 Chapel Hill, North Carolina 27599, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Xin</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Center for Integrative Chemical Biology and Drug Discovery, Division of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, 26 Chapel Hill, North Carolina 27599, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Srimongkolpithak</LastName><ForeName>Nitipol</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Imperial College London, London SW7 2AZ, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jin</LastName><ForeName>Jian</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Center for Integrative Chemical Biology and Drug Discovery, Division of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, 26 Chapel Hill, North Carolina 27599, United States.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Charman</LastName><ForeName>Susan A</ForeName><Initials>SA</Initials><AffiliationInfo><Affiliation>Monash Institute of Pharmaceutical Sciences, 381 Royal Parade, Parkville, Victoria 3052, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Scherf</LastName><ForeName>Artur</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Unité de Biologie des Interactions Hôte-Parasite, Institut Pasteur, F-75724 Paris CEDEX 15, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Centre National de la Recherche Scientifique, Unité de Recherche Associée 2581, F-75724 Paris CEDEX 15, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fuchter</LastName><ForeName>Matthew J</ForeName><Initials>MJ</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Imperial College London, London SW7 2AZ, United Kingdom.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM103893</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01GM103893</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>07</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>ChemMedChem</MedlineTA><NlmUniqueID>101259013</NlmUniqueID><ISSNLinking>1860-7179</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000962">Antimalarials</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011799">Quinazolines</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.43</RegistryNumber><NameOfSubstance UI="D011495">Histone-Lysine N-Methyltransferase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>FEBS Lett. 2011 Jun 6;585(11):1551-62</RefSource><PMID Version="1">21530510</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Med Chem. 2010 Aug 12;53(15):5844-57</RefSource><PMID 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Version="1">21743462</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000962" MajorTopicYN="N">Antimalarials</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011495" MajorTopicYN="N">Histone-Lysine N-Methyltransferase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010963" MajorTopicYN="N">Plasmodium falciparum</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011799" MajorTopicYN="N">Quinazolines</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading></MeshHeadingList><OtherID Source="NLM">NIHMS626793</OtherID><OtherID Source="NLM">PMC4177335</OtherID><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">diaminoquinazolines</Keyword><Keyword MajorTopicYN="N">drug design</Keyword><Keyword MajorTopicYN="N">histone methyltransferase</Keyword><Keyword MajorTopicYN="N">malaria</Keyword><Keyword MajorTopicYN="N">structure-activity relationships</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>04</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>7</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>7</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>5</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25044750</ArticleId><ArticleId IdType="doi">10.1002/cmdc.201402098</ArticleId><ArticleId IdType="pmc">PMC4177335</ArticleId><ArticleId IdType="mid">NIHMS626793</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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