Improved proteolytic stability and potent activity against Leishmania infantum trypanothione reductase of α/β-peptide foldamers conjugated to cell-penetrating peptides.
Identifieur interne : 000B23 ( PubMed/Curation ); précédent : 000B22; suivant : 000B24Improved proteolytic stability and potent activity against Leishmania infantum trypanothione reductase of α/β-peptide foldamers conjugated to cell-penetrating peptides.
Auteurs : Héctor De Lucio [Espagne] ; Ana María Gamo [Espagne] ; Marta Ruiz-Santaquiteria [Espagne] ; Sonia De Castro [Espagne] ; Pedro A. Sánchez-Murcia [Espagne] ; Miguel A. Toro [Espagne] ; Kilian Jesús Gutiérrez [Espagne] ; Federico Gago [Espagne] ; Antonio Jiménez-Ruiz [Espagne] ; María-José Camarasa [Espagne] ; Sonsoles Velázquez [Espagne]Source :
- European journal of medicinal chemistry [ 1768-3254 ] ; 2017.
Descripteurs français
- KwdFr :
- MESH :
- administration et posologie : Peptides de pénétration cellulaire.
- antagonistes et inhibiteurs : NADH, NADPH oxidoreductases.
- enzymologie : Leishmania infantum.
- Animaux, Peptides de pénétration cellulaire, Protéolyse, Séquence d'acides aminés.
English descriptors
- KwdEn :
- MESH :
- chemical , administration & dosage : Cell-Penetrating Peptides.
- chemical , antagonists & inhibitors : NADH, NADPH Oxidoreductases.
- chemical , chemistry : Cell-Penetrating Peptides.
- enzymology : Leishmania infantum.
- Amino Acid Sequence, Animals, Proteolysis.
Abstract
The objective of the current study was to enhance the proteolytic stability of peptide-based inhibitors that target critical protein-protein interactions at the dimerization interface of Leishmania infantum trypanothione reductase (Li-TryR) using a backbone modification strategy. To achieve this goal we carried out the synthesis, proteolytic stability studies and biological evaluation of a small library of α/β3-peptide foldamers of different length (from 9-mers to 13-mers) and different α→β substitution patterns related to prototype linear α-peptides. We show that several 13-residue α/β3-peptide foldamers retain inhibitory potency against the enzyme (in both activity and dimerization assays) while they are far less susceptible to proteolytic degradation than an analogous α-peptide. The strong dependence of the binding affinities for Li-TryR on the length of the α,β-peptides is supported by theoretical calculations on conformational ensembles of the resulting complexes. The conjugation of the most proteolytically stable α/β-peptide with oligoarginines results in a molecule with potent activity against L. infantum promastigotes and amastigotes.
DOI: 10.1016/j.ejmech.2017.09.032
PubMed: 29017116
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Electronic address: iqmsv29@iqm.csic.es.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Instituto de Química Médica (IQM-CSIC), E-28006 Madrid</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2017">2017</date><idno type="RBID">pubmed:29017116</idno><idno type="pmid">29017116</idno><idno type="doi">10.1016/j.ejmech.2017.09.032</idno><idno type="wicri:Area/PubMed/Corpus">000B23</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000B23</idno><idno type="wicri:Area/PubMed/Curation">000B23</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000B23</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Improved proteolytic stability and potent activity against Leishmania infantum trypanothione reductase of α/β-peptide foldamers conjugated to cell-penetrating peptides.</title><author><name sortKey="De Lucio, Hector" sort="De Lucio, Hector" uniqKey="De Lucio H" first="Héctor" last="De Lucio">Héctor De Lucio</name><affiliation wicri:level="1"><nlm:affiliation>Departamento de Biología de Sistemas, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departamento de Biología de Sistemas, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid</wicri:regionArea></affiliation></author><author><name sortKey="Gamo, Ana Maria" sort="Gamo, Ana Maria" uniqKey="Gamo A" first="Ana María" last="Gamo">Ana María Gamo</name><affiliation wicri:level="1"><nlm:affiliation>Instituto de Química Médica (IQM-CSIC), E-28006 Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Instituto de Química Médica (IQM-CSIC), E-28006 Madrid</wicri:regionArea></affiliation></author><author><name sortKey="Ruiz Santaquiteria, Marta" sort="Ruiz Santaquiteria, Marta" uniqKey="Ruiz Santaquiteria M" first="Marta" last="Ruiz-Santaquiteria">Marta Ruiz-Santaquiteria</name><affiliation wicri:level="1"><nlm:affiliation>Instituto de Química Médica (IQM-CSIC), E-28006 Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Instituto de Química Médica (IQM-CSIC), E-28006 Madrid</wicri:regionArea></affiliation></author><author><name sortKey="De Castro, Sonia" sort="De Castro, Sonia" uniqKey="De Castro S" first="Sonia" last="De Castro">Sonia De Castro</name><affiliation wicri:level="1"><nlm:affiliation>Instituto de Química Médica (IQM-CSIC), E-28006 Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Instituto de Química Médica (IQM-CSIC), E-28006 Madrid</wicri:regionArea></affiliation></author><author><name sortKey="Sanchez Murcia, Pedro A" sort="Sanchez Murcia, Pedro A" uniqKey="Sanchez Murcia P" first="Pedro A" last="Sánchez-Murcia">Pedro A. Sánchez-Murcia</name><affiliation wicri:level="1"><nlm:affiliation>Área de Farmacología, Departamento de Ciencias Biomédicas, Unidad Asociada Al IQM-CSIC, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Área de Farmacología, Departamento de Ciencias Biomédicas, Unidad Asociada Al IQM-CSIC, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid</wicri:regionArea></affiliation></author><author><name sortKey="Toro, Miguel A" sort="Toro, Miguel A" uniqKey="Toro M" first="Miguel A" last="Toro">Miguel A. Toro</name><affiliation wicri:level="1"><nlm:affiliation>Departamento de Biología de Sistemas, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departamento de Biología de Sistemas, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid</wicri:regionArea></affiliation></author><author><name sortKey="Gutierrez, Kilian Jesus" sort="Gutierrez, Kilian Jesus" uniqKey="Gutierrez K" first="Kilian Jesús" last="Gutiérrez">Kilian Jesús Gutiérrez</name><affiliation wicri:level="1"><nlm:affiliation>Departamento de Biología de Sistemas, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departamento de Biología de Sistemas, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid</wicri:regionArea></affiliation></author><author><name sortKey="Gago, Federico" sort="Gago, Federico" uniqKey="Gago F" first="Federico" last="Gago">Federico Gago</name><affiliation wicri:level="1"><nlm:affiliation>Área de Farmacología, Departamento de Ciencias Biomédicas, Unidad Asociada Al IQM-CSIC, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Área de Farmacología, Departamento de Ciencias Biomédicas, Unidad Asociada Al IQM-CSIC, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid</wicri:regionArea></affiliation></author><author><name sortKey="Jimenez Ruiz, Antonio" sort="Jimenez Ruiz, Antonio" uniqKey="Jimenez Ruiz A" first="Antonio" last="Jiménez-Ruiz">Antonio Jiménez-Ruiz</name><affiliation wicri:level="1"><nlm:affiliation>Departamento de Biología de Sistemas, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departamento de Biología de Sistemas, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid</wicri:regionArea></affiliation></author><author><name sortKey="Camarasa, Maria Jose" sort="Camarasa, Maria Jose" uniqKey="Camarasa M" first="María-José" last="Camarasa">María-José Camarasa</name><affiliation wicri:level="1"><nlm:affiliation>Instituto de Química Médica (IQM-CSIC), E-28006 Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Instituto de Química Médica (IQM-CSIC), E-28006 Madrid</wicri:regionArea></affiliation></author><author><name sortKey="Velazquez, Sonsoles" sort="Velazquez, Sonsoles" uniqKey="Velazquez S" first="Sonsoles" last="Velázquez">Sonsoles Velázquez</name><affiliation wicri:level="1"><nlm:affiliation>Instituto de Química Médica (IQM-CSIC), E-28006 Madrid, Spain. Electronic address: iqmsv29@iqm.csic.es.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Instituto de Química Médica (IQM-CSIC), E-28006 Madrid</wicri:regionArea></affiliation></author></analytic><series><title level="j">European journal of medicinal chemistry</title><idno type="eISSN">1768-3254</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell-Penetrating Peptides (administration & dosage)</term><term>Cell-Penetrating Peptides (chemistry)</term><term>Leishmania infantum (enzymology)</term><term>NADH, NADPH Oxidoreductases (antagonists & inhibitors)</term><term>Proteolysis</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Leishmania infantum (enzymologie)</term><term>NADH, NADPH oxidoreductases (antagonistes et inhibiteurs)</term><term>Peptides de pénétration cellulaire ()</term><term>Peptides de pénétration cellulaire (administration et posologie)</term><term>Protéolyse</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" type="chemical" qualifier="administration & dosage" xml:lang="en"><term>Cell-Penetrating Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>NADH, NADPH Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cell-Penetrating Peptides</term></keywords><keywords scheme="MESH" qualifier="administration et posologie" xml:lang="fr"><term>Peptides de pénétration cellulaire</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>NADH, NADPH oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Leishmania infantum</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Leishmania infantum</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Proteolysis</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Peptides de pénétration cellulaire</term><term>Protéolyse</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The objective of the current study was to enhance the proteolytic stability of peptide-based inhibitors that target critical protein-protein interactions at the dimerization interface of Leishmania infantum trypanothione reductase (Li-TryR) using a backbone modification strategy. To achieve this goal we carried out the synthesis, proteolytic stability studies and biological evaluation of a small library of α/β<sup>3</sup>-peptide foldamers of different length (from 9-mers to 13-mers) and different α→β substitution patterns related to prototype linear α-peptides. We show that several 13-residue α/β<sup>3</sup>-peptide foldamers retain inhibitory potency against the enzyme (in both activity and dimerization assays) while they are far less susceptible to proteolytic degradation than an analogous α-peptide. The strong dependence of the binding affinities for Li-TryR on the length of the α,β-peptides is supported by theoretical calculations on conformational ensembles of the resulting complexes. The conjugation of the most proteolytically stable α/β-peptide with oligoarginines results in a molecule with potent activity against L. infantum promastigotes and amastigotes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29017116</PMID><DateCompleted><Year>2017</Year><Month>12</Month><Day>01</Day></DateCompleted><DateRevised><Year>2017</Year><Month>12</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1768-3254</ISSN><JournalIssue CitedMedium="Internet"><Volume>140</Volume><PubDate><Year>2017</Year><Month>Nov</Month><Day>10</Day></PubDate></JournalIssue><Title>European journal of medicinal chemistry</Title><ISOAbbreviation>Eur J Med Chem</ISOAbbreviation></Journal><ArticleTitle>Improved proteolytic stability and potent activity against Leishmania infantum trypanothione reductase of α/β-peptide foldamers conjugated to cell-penetrating peptides.</ArticleTitle><Pagination><MedlinePgn>615-623</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0223-5234(17)30746-8</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ejmech.2017.09.032</ELocationID><Abstract><AbstractText>The objective of the current study was to enhance the proteolytic stability of peptide-based inhibitors that target critical protein-protein interactions at the dimerization interface of Leishmania infantum trypanothione reductase (Li-TryR) using a backbone modification strategy. To achieve this goal we carried out the synthesis, proteolytic stability studies and biological evaluation of a small library of α/β<sup>3</sup>-peptide foldamers of different length (from 9-mers to 13-mers) and different α→β substitution patterns related to prototype linear α-peptides. We show that several 13-residue α/β<sup>3</sup>-peptide foldamers retain inhibitory potency against the enzyme (in both activity and dimerization assays) while they are far less susceptible to proteolytic degradation than an analogous α-peptide. The strong dependence of the binding affinities for Li-TryR on the length of the α,β-peptides is supported by theoretical calculations on conformational ensembles of the resulting complexes. The conjugation of the most proteolytically stable α/β-peptide with oligoarginines results in a molecule with potent activity against L. infantum promastigotes and amastigotes.</AbstractText><CopyrightInformation>Copyright © 2017 Elsevier Masson SAS. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>de Lucio</LastName><ForeName>Héctor</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Departamento de Biología de Sistemas, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gamo</LastName><ForeName>Ana María</ForeName><Initials>AM</Initials><AffiliationInfo><Affiliation>Instituto de Química Médica (IQM-CSIC), E-28006 Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ruiz-Santaquiteria</LastName><ForeName>Marta</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Instituto de Química Médica (IQM-CSIC), E-28006 Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>de Castro</LastName><ForeName>Sonia</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Instituto de Química Médica (IQM-CSIC), E-28006 Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sánchez-Murcia</LastName><ForeName>Pedro A</ForeName><Initials>PA</Initials><AffiliationInfo><Affiliation>Área de Farmacología, Departamento de Ciencias Biomédicas, Unidad Asociada Al IQM-CSIC, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Toro</LastName><ForeName>Miguel A</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Departamento de Biología de Sistemas, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gutiérrez</LastName><ForeName>Kilian Jesús</ForeName><Initials>KJ</Initials><AffiliationInfo><Affiliation>Departamento de Biología de Sistemas, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gago</LastName><ForeName>Federico</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Área de Farmacología, Departamento de Ciencias Biomédicas, Unidad Asociada Al IQM-CSIC, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jiménez-Ruiz</LastName><ForeName>Antonio</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Departamento de Biología de Sistemas, Universidad de Alcalá, E-28805 Alcalá de Henares, Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Camarasa</LastName><ForeName>María-José</ForeName><Initials>MJ</Initials><AffiliationInfo><Affiliation>Instituto de Química Médica (IQM-CSIC), E-28006 Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Velázquez</LastName><ForeName>Sonsoles</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Instituto de Química Médica (IQM-CSIC), E-28006 Madrid, Spain. Electronic address: iqmsv29@iqm.csic.es.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>09</Month><Day>21</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="D057846">Cell-Penetrating Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.6.-</RegistryNumber><NameOfSubstance UI="D009247">NADH, NADPH Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.12</RegistryNumber><NameOfSubstance UI="C049608">trypanothione reductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057846" MajorTopicYN="N">Cell-Penetrating Peptides</DescriptorName><QualifierName UI="Q000008" MajorTopicYN="Y">administration & dosage</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018314" MajorTopicYN="N">Leishmania infantum</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009247" MajorTopicYN="N">NADH, NADPH Oxidoreductases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D059748" MajorTopicYN="N">Proteolysis</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Foldamers</Keyword><Keyword MajorTopicYN="N">Leishmania infantum</Keyword><Keyword MajorTopicYN="N">Protein-protein interactions</Keyword><Keyword MajorTopicYN="N">Proteolysis</Keyword><Keyword MajorTopicYN="N">Trypanothione reductase</Keyword><Keyword MajorTopicYN="N">α/β-Peptides</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>07</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2017</Year><Month>08</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2017</Year><Month>09</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>10</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>12</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>10</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29017116</ArticleId><ArticleId IdType="pii">S0223-5234(17)30746-8</ArticleId><ArticleId IdType="doi">10.1016/j.ejmech.2017.09.032</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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