Cyclic Peptide-Based Sirtuin Substrates.
Identifieur interne : 000616 ( PubMed/Checkpoint ); précédent : 000615; suivant : 000617Cyclic Peptide-Based Sirtuin Substrates.
Auteurs : Di Chen [République populaire de Chine] ; Lingling Yan [République populaire de Chine] ; Weiping Zheng [République populaire de Chine]Source :
- Molecules (Basel, Switzerland) [ 1420-3049 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
- analogues et dérivés : Lysine.
- métabolisme : Pronase.
- Acylation, Catalyse, Cinétique, Humains, Lysine, Oxydoréduction, Peptides cycliques, Relation structure-activité, Sirtuines, Structure moléculaire, Thermodynamique.
English descriptors
- KwdEn :
- MESH :
- chemical , analogs & derivatives : Lysine.
- chemical , chemistry : Lysine, Peptides, Cyclic, Sirtuins.
- chemical , metabolism : Pronase.
- Acylation, Catalysis, Humans, Kinetics, Molecular Structure, Oxidation-Reduction, Structure-Activity Relationship, Thermodynamics.
Abstract
In the current study, four side chain-to-side chain cyclic peptides (three 5-mers and one 4-mer) harboring Nε-acetyl-lysine or Nε-myristoyl-lysine were found to be in vitro substrates of the human SIRT1/2/3-catalyzed deacylation with good substrate activities, as judged by the kcat/KM ratios.
DOI: 10.3390/molecules24030424
PubMed: 30682801
Affiliations:
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212013</wicri:noRegion></affiliation></author><author><name sortKey="Yan, Lingling" sort="Yan, Lingling" uniqKey="Yan L" first="Lingling" last="Yan">Lingling Yan</name><affiliation wicri:level="1"><nlm:affiliation>School of Pharmacy, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013, China. 18796012926@163.com.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>School of Pharmacy, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013</wicri:regionArea><wicri:noRegion>Zhenjiang 212013</wicri:noRegion></affiliation></author><author><name sortKey="Zheng, Weiping" sort="Zheng, Weiping" uniqKey="Zheng W" first="Weiping" last="Zheng">Weiping Zheng</name><affiliation wicri:level="1"><nlm:affiliation>School of Pharmacy, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013, China. wzheng@ujs.edu.cn.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>School of Pharmacy, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013</wicri:regionArea><wicri:noRegion>Zhenjiang 212013</wicri:noRegion></affiliation></author></analytic><series><title level="j">Molecules (Basel, Switzerland)</title><idno type="eISSN">1420-3049</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acylation</term><term>Catalysis</term><term>Humans</term><term>Kinetics</term><term>Lysine (analogs & derivatives)</term><term>Lysine (chemistry)</term><term>Molecular Structure</term><term>Oxidation-Reduction</term><term>Peptides, Cyclic (chemistry)</term><term>Pronase (metabolism)</term><term>Sirtuins (chemistry)</term><term>Structure-Activity Relationship</term><term>Thermodynamics</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acylation</term><term>Catalyse</term><term>Cinétique</term><term>Humains</term><term>Lysine ()</term><term>Lysine (analogues et dérivés)</term><term>Oxydoréduction</term><term>Peptides cycliques ()</term><term>Pronase (métabolisme)</term><term>Relation structure-activité</term><term>Sirtuines ()</term><term>Structure moléculaire</term><term>Thermodynamique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Lysine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Lysine</term><term>Peptides, Cyclic</term><term>Sirtuins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Pronase</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Lysine</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Pronase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Acylation</term><term>Catalysis</term><term>Humans</term><term>Kinetics</term><term>Molecular Structure</term><term>Oxidation-Reduction</term><term>Structure-Activity Relationship</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Acylation</term><term>Catalyse</term><term>Cinétique</term><term>Humains</term><term>Lysine</term><term>Oxydoréduction</term><term>Peptides cycliques</term><term>Relation structure-activité</term><term>Sirtuines</term><term>Structure moléculaire</term><term>Thermodynamique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In the current study, four side chain-to-side chain cyclic peptides (three 5-mers and one 4-mer) harboring N<sup>ε</sup>-acetyl-lysine or N<sup>ε</sup>-myristoyl-lysine were found to be in vitro substrates of the human SIRT1/2/3-catalyzed deacylation with good substrate activities, as judged by the <i>k</i><sub>cat</sub>/<i>K</i><sub>M</sub> ratios.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30682801</PMID><DateCompleted><Year>2019</Year><Month>10</Month><Day>07</Day></DateCompleted><DateRevised><Year>2020</Year><Month>02</Month><Day>25</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1420-3049</ISSN><JournalIssue CitedMedium="Internet"><Volume>24</Volume><Issue>3</Issue><PubDate><Year>2019</Year><Month>Jan</Month><Day>24</Day></PubDate></JournalIssue><Title>Molecules (Basel, Switzerland)</Title><ISOAbbreviation>Molecules</ISOAbbreviation></Journal><ArticleTitle>Cyclic Peptide-Based Sirtuin Substrates.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">E424</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.3390/molecules24030424</ELocationID><Abstract><AbstractText>In the current study, four side chain-to-side chain cyclic peptides (three 5-mers and one 4-mer) harboring N<sup>ε</sup>-acetyl-lysine or N<sup>ε</sup>-myristoyl-lysine were found to be in vitro substrates of the human SIRT1/2/3-catalyzed deacylation with good substrate activities, as judged by the <i>k</i><sub>cat</sub>/<i>K</i><sub>M</sub> ratios.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Di</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>School of Pharmacy, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013, China. jsdxchendi@163.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yan</LastName><ForeName>Lingling</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>School of Pharmacy, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013, China. 18796012926@163.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zheng</LastName><ForeName>Weiping</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>School of Pharmacy, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013, China. wzheng@ujs.edu.cn.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>21272094</GrantID><Agency>National Natural Science Foundation of China</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>01</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Molecules</MedlineTA><NlmUniqueID>100964009</NlmUniqueID><ISSNLinking>1420-3049</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010456">Peptides, Cyclic</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.24.-</RegistryNumber><NameOfSubstance UI="D011402">Pronase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.5.1.-</RegistryNumber><NameOfSubstance UI="D037761">Sirtuins</NameOfSubstance></Chemical><Chemical><RegistryNumber>K3Z4F929H6</RegistryNumber><NameOfSubstance UI="D008239">Lysine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000215" MajorTopicYN="N">Acylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008239" MajorTopicYN="N">Lysine</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015394" MajorTopicYN="N">Molecular Structure</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010456" MajorTopicYN="N">Peptides, Cyclic</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011402" MajorTopicYN="N">Pronase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D037761" MajorTopicYN="N">Sirtuins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">cyclic peptide</Keyword><Keyword MajorTopicYN="N">deacylation</Keyword><Keyword MajorTopicYN="N">sirtuin</Keyword><Keyword 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