Effects of Amino Acid Deletion on the Antiplasmodial Activity of Angiotensin II

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dc.contributor.authorRodrigues Ferreira, Luiz Henrique
dc.contributor.authorSilva, Adriana Farias
dc.contributor.authorTorossian Torres, Marcelo Der
dc.contributor.authorPedron, Cibele Nicolaski
dc.contributor.authorCapurro, Margareth Lara
dc.contributor.authorAlves, Flavio Lopes [UNIFESP]
dc.contributor.authorMiranda, Antonio [UNIFESP]
dc.contributor.authorOliveira, Vani Xavier
dc.contributor.institutionUniversidade Federal do ABC (UFABC)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T14:38:14Z
dc.date.available2016-01-24T14:38:14Z
dc.date.issued2014-12-01
dc.description.abstractMalaria is an infectious disease for which effective treatment and prevention strategies remain limited. Our group recently reported that angiotensin II (AII) presents antiplasmodial activity and inhibits the development of Plasmodium gallinaceum in Aedes aegypti. However, details concerning role of each amino acid residue in the antiplasmodial activity of the peptide and information about the minimal structure responsible for this activity remain unknown. in this work, we investigated the effects of specific deletions (i.e., mono-, di-, tri- and tetra-deletions) of AII amino acids on the antiplasmodial activity of this molecule. the peptides were synthesized on solid phase method using the t-Boc strategy, purified using high performance liquid chromatography and characterized using mass spectrometry. the lytic activity of the peptides was assessed in vitro using mature sporozoites extracted from the salivary glands of infected Aedes aegypti mosquitoes. the results demonstrate that all of the deletions reduced antiplasmodial activity compared to native AII and that active analogs tend to adopt beta-turn conformations; however, the deletion of bulky hydrophobic residues causes greater reductions of bioactivity than the deletion of hydrophilic residues. Corroborating previous studies, we observed that analog extremities are susceptible to changes and can be carefully modified without compromising the activity of this compound. This research contributes to our understanding of the role of each AII amino acid residue in activity against Plasmodium gallinaceum and identifies two short analogs with similar antiplasmodial activity to AII. These analogs may be candidates for additional antimalarial assays because they are inexpensive and easy to synthesize.en
dc.description.affiliationUniv Fed ABC, Ctr Ciencias Nat & Humanas, BR-09210170 Santo Andre, SP, Brazil
dc.description.affiliationUniv São Paulo, Inst Ciencias Biomed, BR-05508 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biofis, São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biofis, São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipIDFAPESP: 2008/51869-9
dc.description.sponsorshipIDFAPESP: 2011/10823-9
dc.description.sponsorshipIDFAPESP: 2011/15083-3
dc.description.sponsorshipIDFAPESP: 2011/11448-2
dc.format.extent553-564
dc.identifierhttp://dx.doi.org/10.1007/s10989-014-9425-9
dc.identifier.citationInternational Journal of Peptide Research and Therapeutics. New York: Springer, v. 20, n. 4, p. 553-564, 2014.
dc.identifier.doi10.1007/s10989-014-9425-9
dc.identifier.issn1573-3149
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/38497
dc.identifier.wosWOS:000344349900018
dc.language.isoeng
dc.publisherSpringer
dc.relation.ispartofInternational Journal of Peptide Research and Therapeutics
dc.rightsAcesso restrito
dc.rights.licensehttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dc.subjectMalariaen
dc.subjectAngiotensin IIen
dc.subjectSporozoitesen
dc.subjectPlasmodium gallinaceumen
dc.subjectSPPSen
dc.subjectStructure-activity relationshipen
dc.titleEffects of Amino Acid Deletion on the Antiplasmodial Activity of Angiotensin IIen
dc.typeArtigo
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