Structure optimization of lipopeptide assemblies for aldol reactions in an aqueous medium

dc.citation.volume23pt_BR
dc.contributor.authorda Silva, Emerson Rodrigo [UNIFESP]
dc.contributor.authorSoares, Bruna Miranda
dc.contributor.authorSodré, Pedro
dc.contributor.authorArguello, Karina
dc.contributor.authorAguilar, Andrea
dc.contributor.authorPelin, Juliane
dc.contributor.authorGerbelli, Barbara Bianca
dc.contributor.authorSchmuck, Carsten
dc.contributor.authorFarias, Marcelo
dc.contributor.authorPortugal, Rodrigo
dc.contributor.authorCoutinho-Neto, Maurício
dc.contributor.authorAlves, Wendel Andrade
dc.contributor.authorLatteshttp://lattes.cnpq.br/7800589206457326pt_BR
dc.date.accessioned2023-05-11T13:12:13Z
dc.date.available2023-05-11T13:12:13Z
dc.date.issued2021-03-09
dc.description.abstractFour amphiphilic peptides were synthesized, characterized, and evaluated regarding their efficiency in the catalysis of direct aldol reactions in water. The lipopeptides differ by having a double lipid chain and a guanidinium pyrrole group functionalizing one Lys side chain. All the samples are composed of the amino acids L-proline (P), L-arginine (R), or L-lysine (K) functionalized with the cationic guanidiniocarbonyl pyrrole unit (GCP), L-tryptophan (W), and L-glycine (G), covalently linked to one or two long aliphatic chains, leading to surfactant-like designs with controlled proline protonation state and different stereoselectivity. Critical aggregation concentrations (cac) were higher in the presence of the GCP group, suggesting that self-assembly depends on charge distribution along the peptide backbone. Cryogenic Transmission Electron Microscopy (Cryo-TEM) and Small Angle X-ray Scattering (SAXS) showed a rich polymorphism including spherical, cylindrical, and bilayer structures. Molecular dynamics simulations performed to assess the lipopeptide polymorphs revealed an excellent agreement with core-shell arrangements derived from SAXS data and provided an atomistic view of the changes incurred by modifying head groups and lipid chains. The resulting nanostructures behaved as excellent catalysts for aldol condensation reactions, in which superior conversions (>99%), high diastereoselectivities (ds = 94:6), and enantioselectivities (ee = 92%) were obtained. Our findings contribute to elucidate the effect of nanoscale organization of lipopeptide assemblies in the catalysis of aldol reactions in an aqueous environment.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipID19/20907-7pt_BR
dc.format.extent10953pt_BR
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/67485
dc.languageengpt_BR
dc.publisherRoyal Society of Chemistryen
dc.relation.ispartofPhysical Chemistry Chemical Physicsen
dc.rightsAcesso abertopt_BR
dc.subjectSelf-assemblyen
dc.subjectLipopeptidesen
dc.subjectCatalysisen
dc.subjectStructureen
dc.titleStructure optimization of lipopeptide assemblies for aldol reactions in an aqueous mediumen
dc.typeArtigopt_BR
unifesp.campusEscola Paulista de Medicina (EPM)pt_BR
unifesp.departamentoBiofísicapt_BR
unifesp.graduateProgramCiências Biológicas (Biologia Molecular)pt_BR
unifesp.knowledgeAreaBiofísicapt_BR
unifesp.researchAreaBiofísica molecularpt_BR
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