N-Terminal microdomain peptide from human dihydroorotate dehydrogenase: structure and model membrane interactions

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dc.contributor.authorVicente, Eduardo F. [UNESP]
dc.contributor.authorNobre-Pavinatto, Thatyane M. [UNESP]
dc.contributor.authorPavinatto, Felippe J. [UNESP]
dc.contributor.authorOliveira Junior, Osvaldo Natale [UNESP]
dc.contributor.authorCosta-filho, Antonio J. da [UNESP]
dc.contributor.authorCilli, Eduardo Maffud [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2015-05-15T13:30:16Z
dc.date.available2015-05-15T13:30:16Z
dc.date.issued2014
dc.description.abstractThe N-terminus of the human dihydroorotate dehydrogenase (HsDHODH) has been described as important for the enzyme attachment in the inner mitochondrial membrane and possibly to regulate enzymatic activity. In this study, we synthesized the peptide acetyl-GDERFYAEHLMPTLQGLLDPESAHRL AVRFTSLGamide, comprising the residues 33-66 of HsDHODH N-terminal conserved microdomain. Langmuir monolayers and circular dichroism (CD) were employed to investigate the interactions between the peptide and membrane model, as micelles and monolayers of the lipids phosphatidylcholine (PC), 3-phosphatidylethanolamine (PE) and cardiolipin (CL). These lipids represent the major constituents of inner mitochondrial membranes. According to CD data, the peptide adopted a random structure in water, whereas it acquired α-helical structures in the presence of micelles. The π–A isotherms and polarization- modulated infrared reflection-absorption spectroscopy on monolayers showed that the peptide interacted with all lipids, but in different ways. In DPPC monolayers, the peptide penetrated into the hydrophobic region. The strongest initial interaction occurred with DPPE, but the peptide was expelled from this monolayer at high surface pressures. In CL, the peptide could induce a partial dissolution of the monolayer, leading to shorter areas at the monolayer collapse. These results corroborate the literature, where the HsDHODH microdomain is anchored into the inner mitochondrial membrane. Moreover, the existence of distinct conformations and interactions with the different membrane lipids indicates that the access to the enzyme active site may be controlled not only by conformational changes occurring at the microdomain of the protein, but also by some lipid-protein synergetic mechanism, where the HsDHODH peptide would be able to recognize lipid domains in the membrane. - See more at: http://www.eurekaselect.com/122062/article#sthash.1ZZbc7E0.dpufen
dc.description.affiliationUniversidade Estadual Paulista Júlio de Mesquita Filho, Departamento de Bioquímica e Tecnologia Química, Instituto de Química de Araraquara, Araraquara, Rua Professor Francisco Degni, 55, Jardim Quitandinha, CEP 14800060, SP, Brasil
dc.description.affiliationUnespUniversidade Estadual Paulista Júlio de Mesquita Filho, Departamento de Bioquímica e Tecnologia Química, Instituto de Química de Araraquara, Araraquara, Rua Professor Francisco Degni, 55, Jardim Quitandinha, CEP 14800060, SP, Brasil
dc.format.extent119-129
dc.identifier.citationProtein and Peptide Letters, v. 22, n. 2, p. 119-129, 2014.
dc.identifier.doi10.2174/0929866521666140508125215
dc.identifier.issn0929-8665
dc.identifier.lattes9424346762460416
dc.identifier.orcid0000-0002-4767-0904
dc.identifier.urihttp://hdl.handle.net/11449/123474
dc.language.isoeng
dc.relation.ispartofProtein and Peptide Letters
dc.relation.ispartofjcr1.039
dc.relation.ispartofsjr0,429
dc.rights.accessRightsAcesso restrito
dc.sourceCurrículo Lattes
dc.subjectCircular dichroismen
dc.subjectHuman dihydroorotate dehydrogenaseen
dc.subjectLangmuir monolayersen
dc.subjectpeptideen
dc.subjectPhospholipidsen
dc.subjectPolarization- modulated infrared reflection-absorption spectroscopyen
dc.subjectOlid-phase peptide synthesisen
dc.titleN-Terminal microdomain peptide from human dihydroorotate dehydrogenase: structure and model membrane interactionsen
dc.typeArtigo
unesp.author.lattes9424346762460416
unesp.author.lattes6380599830437803[1]
unesp.author.orcid0000-0002-4767-0904[6]
unesp.author.orcid0000-0002-9154-3574[1]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Química, Araraquarapt
unesp.departmentBioquímica e Tecnologia Químicapt

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