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Catalytic peptide-based coacervates for enhanced function through structural organization and substrate specificity

2024-10-30Artigo científico Acesso aberto
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dc.contributor.authorReis, David Q.P.
dc.contributor.authorPereira, Sara
dc.contributor.authorRamos, Ana P.
dc.contributor.authorPereira, Pedro M.
dc.contributor.authorMorgado, Leonor
dc.contributor.authorCalvário, Joana
dc.contributor.authorHenriques, Adriano O.
dc.contributor.authorSerrano, Mónica
dc.contributor.authorPina, Ana S.
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.contributor.institutionFaculdade de Ciências e Tecnologia (FCT)
dc.contributor.pblNature Portfolio
dc.date.accessioned2025-02-06T21:19:55Z
dc.date.available2025-02-06T21:19:55Z
dc.date.issued2024-10-30
dc.descriptionThis work was partially supported by PPBI - Portuguese Platform of BioImaging (PPBI-POCI-01-0145-FEDER-022122) co-funded by national funds from OE - \u201COr\u00E7amento de Estado\u201D and by european funds from FEDER - \u201CFundo Europeu de Desenvolvimento Regional. La Caixa Junior Leader Fellowship (LCF/BQ/PI20/11760012) financed by\u201Dla Caixa\u201D Foundation (ID 100010434) and a Maratona da Sa\u00FAde award. The NMR spectrometers at CERMAX, ITQB-NOVA, Oeiras are funded by FCT through project AAC 01/SAICT/2016, while those from FCT-NOVA are part of the National NMR Network and are supported by FCT (ROTEIRO/0031/2013) cofounded by FEDER through COMPETE 2020, POCI, PORL and FCT through PIDDAC. Publisher Copyright: © The Author(s) 2024.
dc.description.abstractLiquid-liquid phase separation (LLPS) in living cells provides innovative pathways for synthetic compartmentalized catalytic systems. While LLPS has been explored for enhancing enzyme catalysis, its potential application to catalytic peptides remains unexplored. Here, we demonstrate the use of coacervation, a key LLPS feature, to constrain the conformational flexibility of catalytic peptides, resulting in structured domains that enhance peptide catalysis. Using the flexible catalytic peptide P7 as a model, we induce reversible biomolecular coacervates with structured peptide domains proficient in hydrolyzing phosphate ester molecules and selectively sequestering phosphorylated proteins. Remarkably, these coacervate-based microreactors exhibit a 15,000-fold increase in catalytic efficiency compared to soluble peptides. Our findings highlight the potential of a single peptide to induce coacervate formation, selectively recruit substrates, and mediate catalysis, enabling a simple design for low-complexity, single peptide-based compartments with broad implications. Moreover, LLPS emerges as a fundamental mechanism in the evolution of chemical functions, effectively managing conformational heterogeneity in short peptides and providing valuable insights into the evolution of enzyme activity and catalysis in prebiotic chemistry.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent2093500
dc.identifier.doi10.1038/s41467-024-53699-z
dc.identifier.issn2041-1723
dc.identifier.otherPURE: 107717056
dc.identifier.otherPURE UUID: 60c8c08c-7350-43a2-915f-3f978f46276c
dc.identifier.otherScopus: 85208162986
dc.identifier.otherPubMed: 39477955
dc.identifier.otherWOS: 001346144300029
dc.identifier.otherORCID: /0000-0001-9729-0371/work/177534525
dc.identifier.otherORCID: /0000-0002-3760-5180/work/177535977
dc.identifier.urihttp://hdl.handle.net/10362/178560
dc.identifier.urlhttps://www.scopus.com/pages/publications/85208162986
dc.language.isoeng
dc.peerreviewedyes
dc.relationFunding Information: info:eu-repo/grantAgreement/FCT/OE/UI%2FBD%2F154577%2F2022/PT
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dc.relationPeptide-PARC: Programmable Coacervation of short peptides into Artificial Regulatory Compartments
dc.relationInvestigating the mechanisms underpinning the interaction between autonomous immunity and intracellular S. aureus cell division and persistence.
dc.relationJunior Leader la Caixa Postdoctoral Fellowship Programme: Shaping the new generation of leaders in research
dc.relationRedoxMaze – Understanding bacterial extracellular electron transfer for sustainable bio-based solutions
dc.relationApplied Molecular Biosciences Unit
dc.relationApplied Molecular Biosciences Unit
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F04378%2F2020/PT
dc.relationPortuguese Nuclear Magnetic Resonance Network
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04378%2F2020/PT
dc.relationinfo:eu-repo/grantAgreement/FCT/Concurso para Atribuição do Estatuto e Financiamento de Laboratórios Associados (LA)/LA%2FP%2F0140%2F2020/PT
dc.relationinfo:eu-repo/grantAgreement/FCT/9444 - RNIIIE/PINFRA%2F22161%2F2016/PT
dc.subjectGeneral Chemistry
dc.subjectGeneral Biochemistry,Genetics and Molecular Biology
dc.subjectGeneral Physics and Astronomy
dc.titleCatalytic peptide-based coacervates for enhanced function through structural organization and substrate specificityen
dc.typejournal article
degois.publication.issue1
degois.publication.titleNature Communications
degois.publication.volume15
dspace.entity.typePublication
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oaire.awardTitlePeptide-PARC: Programmable Coacervation of short peptides into Artificial Regulatory Compartments
oaire.awardTitleInvestigating the mechanisms underpinning the interaction between autonomous immunity and intracellular S. aureus cell division and persistence.
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