Evidences for the action mechanism of angiotensin II and its analogs on Plasmodium sporozoite membranes

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dc.citation.issue3
dc.citation.volume22
dc.contributor.authorTorossian Torres, Marcelo Der
dc.contributor.authorSilva, Adriana Farias
dc.contributor.authorAlves, Flavio Lopes [UNIFESP]
dc.contributor.authorCapurro, Margareth Lara
dc.contributor.authorMiranda, Antonio [UNIFESP]
dc.contributor.authorCordeiro, Rodrigo Maghdissian
dc.contributor.authorOliveira Junior, Vani Xavier
dc.coverageHoboken
dc.date.accessioned2020-08-21T17:00:19Z
dc.date.available2020-08-21T17:00:19Z
dc.date.issued2016
dc.description.abstractMalaria is an infectious disease responsible for approximately one million deaths annually. Oligopeptides such as angiotensin II (AII) and its analogs are known to have antimalarial effects against Plasmodium gallinaceum and Plasmodium falciparum. However, their mechanism of action is still not fully understood at the molecular level. In the work reported here, we investigated this issue by comparing the antimalarial activity of AII with that of (i) its diastereomer formed by only d-amino acids; (ii) its isomer with reversed sequence; and (iii) its analogs restricted by lactam bridges, the so-called VC5 peptides. Data from fluorescence spectroscopy indicated that the antiplasmodial activities of both all-D-AII and all-D-VC5 were as high as those of the related peptides AII and VC5, respectively. In contrast, retro-AII had no significant effect against P. gallinaceum. Conformational analysis by circular dichroism suggested that AII and its active analogs usually adopted a -turn conformation in different solutions. In the presence of membrane-mimetic micelles, AII had also a -turn conformation, while retro-AII was random. Molecular dynamics simulations demonstrated that the AII chains were slightly more bent than retro-AII at the surface of a model membrane. At the hydrophobic membrane interior, however, the retro-AII chain was severely coiled and rigid. AII was much more flexible and able to experience both straight and coiled conformations. We took it as an indication of the stronger ability of AII to interact with membrane headgroups and promote pore formation. Copyright (c) 2016 European Peptide Society and John Wiley & Sons, Ltd.en
dc.description.affiliationUniv Fed ABC, Ctr Ciencias Nat & Humanas, Rua Santa Adelia 166, Santo Andre, SP, Brazil
dc.description.affiliationUniv Fed Sao Paulo, Dept Biofis, Sao Paulo, SP, Brazil
dc.description.affiliationUniv Sao Paulo, Inst Ciencias Biomed 2, Sao Paulo, SP, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, Dept Biofis, Sao Paulo, SP, Brazil
dc.description.sourceWeb of Science
dc.format.extent132-142
dc.identifierhttp://dx.doi.org/10.1002/psc.2849
dc.identifier.citationJournal Of Peptide Science. Hoboken, v. 22, n. 3, p. 132-142, 2016.
dc.identifier.doi10.1002/psc.2849
dc.identifier.issn1075-2617
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/57938
dc.identifier.wosWOS:000370220200001
dc.language.isoeng
dc.publisherWiley
dc.relation.ispartofJournal Of Peptide Science
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectangiotensin IIen
dc.subjectmalariaen
dc.subjectmolecular dynamicsen
dc.subjectPlasmodiumen
dc.titleEvidences for the action mechanism of angiotensin II and its analogs on Plasmodium sporozoite membranesen
dc.typeinfo:eu-repo/semantics/article
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