Highly Potential Antiplasmodial Restricted Peptides

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dc.contributor.authorDer Torossian, Torres Marcelo
dc.contributor.authorSilva, Adriana F.
dc.contributor.authorAlves, Flavio L. [UNIFESP]
dc.contributor.authorCapurro, Margareth L.
dc.contributor.authorMiranda, Antonio [UNIFESP]
dc.contributor.authorXavier, Oliveira Vani
dc.contributor.institutionUniversidade Federal do ABC (UFABC)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2016-01-24T14:40:01Z
dc.date.available2016-01-24T14:40:01Z
dc.date.issued2015-02-01
dc.description.abstractMalaria is an infectious disease responsible for approximately one million deaths annually. the antimalarial effects of angiotensin II and its analogs against Plasmodium gallinaceum and P.falciparum have recently been reported. To evaluate antiplasmodial activity, we synthesized five angiotensin II-restricted analogs containing disulfide bridges. To accomplish this, peptides containing two inserted amino acid residues (cysteine) were synthesized by the Fmoc solid-phase method, purified by liquid chromatography, and characterized by mass spectrometry. Conformational studies were performed by circular dichroism. the results indicated that two of the analogs had higher antiplasmodium activity (92% and 98% activity) than angiotensin II (88% activity), measured by fluorescence microscopy. Results showed that the insertion position must be selected, to preserve the hydrophobic interactions between the non-polar residues, as this affects antiplasmodial activity. the circular dichroism studies suggested that the active analogs as well as the native angiotensin II adopt a -turn conformation in different solutions. This approach provided insight for understanding the effects of restricting the ring size and position on the bioactivity of angiotensin II and provides a new direction for the design of potential chemotherapeutic agents.en
dc.description.affiliationUniv Fed ABC, Ctr Ciencias Nat & Humanas, Santo Andre, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biofis, São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Inst Ciencias Biomed 2, São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biofis, São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipIDFAPESP: 2011/10823-9
dc.description.sponsorshipIDFAPESP: 2011/15083-3
dc.description.sponsorshipIDFAPESP: 2011/11448-2
dc.format.extent163-171
dc.identifierhttp://dx.doi.org/10.1111/cbdd.12354
dc.identifier.citationChemical Biology & Drug Design. Hoboken: Wiley-Blackwell, v. 85, n. 2, p. 163-171, 2015.
dc.identifier.doi10.1111/cbdd.12354
dc.identifier.issn1747-0277
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/38727
dc.identifier.wosWOS:000347890900007
dc.language.isoeng
dc.publisherWiley-Blackwell
dc.relation.ispartofChemical Biology & Drug Design
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dc.subjectangiotensin IIen
dc.subjectdisulfide bridgeen
dc.subjectmalariaen
dc.subjectPlasmodiumen
dc.subjectSARen
dc.titleHighly Potential Antiplasmodial Restricted Peptidesen
dc.typeinfo:eu-repo/semantics/article
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