The use of nanopore analysis for discovering drugs which bind to α-synuclein for treatment of Parkinson's disease.
Identifieur interne : 001859 ( Ncbi/Merge ); précédent : 001858; suivant : 001860The use of nanopore analysis for discovering drugs which bind to α-synuclein for treatment of Parkinson's disease.
Auteurs : Omid Tavassoly [Canada] ; Joe Kakish [Canada] ; Sergiy Nokhrin [Canada] ; Oleg Dmitriev [Canada] ; Jeremy S. Lee [Canada]Source :
- European journal of medicinal chemistry [ 1768-3254 ] ; 2014.
English descriptors
- KwdEn :
- Binding Sites, Biological Products (chemistry), Biological Products (isolation & purification), Biological Products (metabolism), Biological Products (therapeutic use), Caffeine (chemistry), Caffeine (metabolism), Calorimetry, Drug Discovery (methods), Humans, Molecular Conformation, Nanopores, Nicotine (analogs & derivatives), Nicotine (chemistry), Nicotine (metabolism), Nuclear Magnetic Resonance, Biomolecular, Parkinson Disease (drug therapy), Protein Folding, Structure-Activity Relationship, alpha-Synuclein (antagonists & inhibitors), alpha-Synuclein (metabolism).
- MESH :
- chemical , analogs & derivatives : Nicotine.
- chemical , antagonists & inhibitors : alpha-Synuclein.
- chemical , chemistry : Biological Products, Caffeine, Nicotine.
- chemical , isolation & purification : Biological Products.
- chemical , metabolism : Biological Products, Caffeine, Nicotine, alpha-Synuclein.
- chemical , therapeutic use : Biological Products.
- drug therapy : Parkinson Disease.
- methods : Drug Discovery.
- Binding Sites, Calorimetry, Humans, Molecular Conformation, Nanopores, Nuclear Magnetic Resonance, Biomolecular, Protein Folding, Structure-Activity Relationship.
Abstract
A major feature of Parkinson's disease is the formation of Lewy bodies in dopaminergic neurons which consist of misfolded α-synuclein. The binding of natural products to α-synuclein was evaluated by nanopore analysis and caffeine, curcumin, and nicotine all caused large conformational changes which may be related to their known neuroprotective effect in Parkinson's disease. The binding of the stereoisomers of nicotine were also studied by ITC, CD and NMR. It is proposed that (-)-nicotine causes the folding of α-synuclein into a loop with interaction between the N- and C-termini. For (+)-nicotine the binding is weaker and mainly involves residues in the N-terminus. Caffeine and nicotine can bind to α-synuclein simultaneously and may provide lead structures for the development of other compounds for the treatment of PD.
DOI: 10.1016/j.ejmech.2014.07.090
PubMed: 25081642
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pubmed:25081642Le document en format XML
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Lee</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, 107 Wiggins Road, University of Saskatchewan, Saskatoon, Canada S7N 0W0. Electronic address: jeremy.lee@usask.ca.</nlm:affiliation><country>Canada</country><wicri:regionArea>Department of Biochemistry, 107 Wiggins Road, University of Saskatchewan, Saskatoon</wicri:regionArea><wicri:noRegion>Saskatoon</wicri:noRegion></affiliation></author></analytic><series><title level="j">European journal of medicinal chemistry</title><idno type="eISSN">1768-3254</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites</term><term>Biological Products (chemistry)</term><term>Biological Products (isolation & purification)</term><term>Biological Products (metabolism)</term><term>Biological Products (therapeutic use)</term><term>Caffeine (chemistry)</term><term>Caffeine (metabolism)</term><term>Calorimetry</term><term>Drug Discovery (methods)</term><term>Humans</term><term>Molecular Conformation</term><term>Nanopores</term><term>Nicotine (analogs & derivatives)</term><term>Nicotine (chemistry)</term><term>Nicotine (metabolism)</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Parkinson Disease (drug therapy)</term><term>Protein Folding</term><term>Structure-Activity Relationship</term><term>alpha-Synuclein (antagonists & inhibitors)</term><term>alpha-Synuclein (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Nicotine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Biological Products</term><term>Caffeine</term><term>Nicotine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Biological Products</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Biological Products</term><term>Caffeine</term><term>Nicotine</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="therapeutic use" xml:lang="en"><term>Biological Products</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Drug Discovery</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Calorimetry</term><term>Humans</term><term>Molecular Conformation</term><term>Nanopores</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Protein Folding</term><term>Structure-Activity Relationship</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A major feature of Parkinson's disease is the formation of Lewy bodies in dopaminergic neurons which consist of misfolded α-synuclein. The binding of natural products to α-synuclein was evaluated by nanopore analysis and caffeine, curcumin, and nicotine all caused large conformational changes which may be related to their known neuroprotective effect in Parkinson's disease. The binding of the stereoisomers of nicotine were also studied by ITC, CD and NMR. It is proposed that (-)-nicotine causes the folding of α-synuclein into a loop with interaction between the N- and C-termini. For (+)-nicotine the binding is weaker and mainly involves residues in the N-terminus. Caffeine and nicotine can bind to α-synuclein simultaneously and may provide lead structures for the development of other compounds for the treatment of PD.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25081642</PMID><DateCreated><Year>2014</Year><Month>12</Month><Day>03</Day></DateCreated><DateCompleted><Year>2015</Year><Month>08</Month><Day>27</Day></DateCompleted><DateRevised><Year>2015</Year><Month>11</Month><Day>19</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1768-3254</ISSN><JournalIssue CitedMedium="Internet"><Volume>88</Volume><PubDate><Year>2014</Year><Month>Dec</Month><Day>17</Day></PubDate></JournalIssue><Title>European journal of medicinal chemistry</Title><ISOAbbreviation>Eur J Med Chem</ISOAbbreviation></Journal><ArticleTitle>The use of nanopore analysis for discovering drugs which bind to α-synuclein for treatment of Parkinson's disease.</ArticleTitle><Pagination><MedlinePgn>42-54</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ejmech.2014.07.090</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0223-5234(14)00705-3</ELocationID><Abstract><AbstractText>A major feature of Parkinson's disease is the formation of Lewy bodies in dopaminergic neurons which consist of misfolded α-synuclein. The binding of natural products to α-synuclein was evaluated by nanopore analysis and caffeine, curcumin, and nicotine all caused large conformational changes which may be related to their known neuroprotective effect in Parkinson's disease. The binding of the stereoisomers of nicotine were also studied by ITC, CD and NMR. It is proposed that (-)-nicotine causes the folding of α-synuclein into a loop with interaction between the N- and C-termini. For (+)-nicotine the binding is weaker and mainly involves residues in the N-terminus. Caffeine and nicotine can bind to α-synuclein simultaneously and may provide lead structures for the development of other compounds for the treatment of PD.</AbstractText><CopyrightInformation>Crown Copyright © 2014. Published by Elsevier Masson SAS. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tavassoly</LastName><ForeName>Omid</ForeName><Initials>O</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, 107 Wiggins Road, University of Saskatchewan, Saskatoon, Canada S7N 0W0.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kakish</LastName><ForeName>Joe</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, 107 Wiggins Road, University of Saskatchewan, Saskatoon, Canada S7N 0W0.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nokhrin</LastName><ForeName>Sergiy</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, 107 Wiggins Road, University of Saskatchewan, Saskatoon, Canada S7N 0W0.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dmitriev</LastName><ForeName>Oleg</ForeName><Initials>O</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, 107 Wiggins Road, University of Saskatchewan, Saskatoon, Canada S7N 0W0.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Jeremy S</ForeName><Initials>JS</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, 107 Wiggins Road, University of Saskatchewan, Saskatoon, Canada S7N 0W0. Electronic address: jeremy.lee@usask.ca.</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>07</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>France</Country><MedlineTA>Eur J Med Chem</MedlineTA><NlmUniqueID>0420510</NlmUniqueID><ISSNLinking>0223-5234</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001688">Biological Products</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051844">alpha-Synuclein</NameOfSubstance></Chemical><Chemical><RegistryNumber>3G6A5W338E</RegistryNumber><NameOfSubstance UI="D002110">Caffeine</NameOfSubstance></Chemical><Chemical><RegistryNumber>6M3C89ZY6R</RegistryNumber><NameOfSubstance UI="D009538">Nicotine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001688" MajorTopicYN="N">Biological Products</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000627" MajorTopicYN="N">therapeutic use</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002110" MajorTopicYN="N">Caffeine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002151" MajorTopicYN="N">Calorimetry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055808" MajorTopicYN="N">Drug Discovery</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008968" MajorTopicYN="N">Molecular Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D058608" MajorTopicYN="Y">Nanopores</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009538" MajorTopicYN="N">Nicotine</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019906" MajorTopicYN="N">Nuclear Magnetic Resonance, Biomolecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="Y">drug therapy</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="N">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051844" MajorTopicYN="N">alpha-Synuclein</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Caffeine</Keyword><Keyword MajorTopicYN="N">Curcumin</Keyword><Keyword MajorTopicYN="N">Induced folding</Keyword><Keyword MajorTopicYN="N">Intrinsically disordered protein</Keyword><Keyword MajorTopicYN="N">Nanopore analysis</Keyword><Keyword MajorTopicYN="N">Nicotine</Keyword><Keyword MajorTopicYN="N">Parkinson's disease</Keyword><Keyword MajorTopicYN="N">α-Synuclein</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>04</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>07</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>07</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>8</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>8</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>8</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25081642</ArticleId><ArticleId IdType="pii">S0223-5234(14)00705-3</ArticleId><ArticleId IdType="doi">10.1016/j.ejmech.2014.07.090</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country></list><tree><country name="Canada"><noRegion><name sortKey="Tavassoly, Omid" sort="Tavassoly, Omid" uniqKey="Tavassoly O" first="Omid" last="Tavassoly">Omid Tavassoly</name></noRegion><name sortKey="Dmitriev, Oleg" sort="Dmitriev, Oleg" uniqKey="Dmitriev O" first="Oleg" last="Dmitriev">Oleg Dmitriev</name><name sortKey="Kakish, Joe" sort="Kakish, Joe" uniqKey="Kakish J" first="Joe" last="Kakish">Joe Kakish</name><name sortKey="Lee, Jeremy S" sort="Lee, Jeremy S" uniqKey="Lee J" first="Jeremy S" last="Lee">Jeremy S. Lee</name><name sortKey="Nokhrin, Sergiy" sort="Nokhrin, Sergiy" uniqKey="Nokhrin S" first="Sergiy" last="Nokhrin">Sergiy Nokhrin</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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