New proline-rich oligopeptides from the venom of African adders: Insights into the hypotensive effect of the venoms

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dc.contributor.author Kodama, Roberto T.
dc.contributor.author Cajado-Carvalho, Daniela
dc.contributor.author Kuniyoshi, Alexandre K.
dc.contributor.author Kitano, Eduardo S.
dc.contributor.author Tashima, Alexandre K. [UNIFESP]
dc.contributor.author Barna, Barbara F.
dc.contributor.author Takakura, Ana Carolina
dc.contributor.author Serrano, Solange M. T.
dc.contributor.author Dias-Da-Silva, Wilmar
dc.contributor.author Tambourgi, Denise V.
dc.contributor.author Portaro, Femanda V.
dc.date.accessioned 2016-01-24T14:40:33Z
dc.date.available 2016-01-24T14:40:33Z
dc.date.issued 2015-06-01
dc.identifier http://dx.doi.org/10.1016/j.bbagen.2015.02.005
dc.identifier.citation Biochimica Et Biophysica Acta-general Subjects. Amsterdam: Elsevier B.V., v. 1850, n. 6, p. 1180-1187, 2015.
dc.identifier.issn 0304-4165
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/39122
dc.description.abstract Background: the snakes from the Bitis genus are some of the most medically important venomous snakes in sub Saharan Africa, however little is known about the composition and effects of these snake venom peptides. Considering that the victims with Bids genus snakes have exacerbate hypotension and cardiovascular disorders, we investigated here the presence of angiotensin-converting enzyme modulators on four different species of venoms.Methods: the peptide fractions from Bids gabonica gabonica, Bids nasicornis, Bids gabonica rhinoceros and Bitis arietans which showed inhibitory activity on angiotensin-converting enzyme were subjected to mass spectrometry analysis. Eight proline-rich peptides were synthetized and their potencies were evaluated in vitro and in vivo.Results: the MS analysis resulted in over 150 sequences, out of which 32 are new praline-rich oligopeptides, and eight were selected for syntheses. for some peptides, inhibition assays showed inhibitory potentials of cleavage of angiotensin I ten times greater when compared to bradykinin. in vivo tests showed that all peptides decreased mean arterial pressure, followed by tachycardia in 6 out of 8 of the tests.Conclusion: We describe here some new and already known praline-rich peptides, also known as bradykininpotentiating peptides. Four synthetic peptides indicated a preferential inhibition of angiotensin-converting enzyme C-domain. in vivo studies show that the praline-rich oligopeptides are hypotensive molecules.General significance: Although praline-rich oligopeptides are known molecules, we present here 32 new sequences that are inhibitors of the angiotensin-converting enzyme and consistent with the symptoms of the victims of Bids spp, who display severe hypotension. (C) 2015 Elsevier B.V. All rights reserved. en
dc.description.sponsorship Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorship Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorship Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent 1180-1187
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof Biochimica Et Biophysica Acta-general Subjects
dc.rights Acesso restrito
dc.subject Bitis en
dc.subject Venom en
dc.subject Praline-rich oligopeptide (PRO) en
dc.subject Bradykinin-potentiating peptide (BPP) en
dc.subject Angiotensin-converting enzyme (ACE) en
dc.subject Hypotension en
dc.title New proline-rich oligopeptides from the venom of African adders: Insights into the hypotensive effect of the venoms en
dc.type Artigo
dc.rights.license http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institution Butantan Inst
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.contributor.institution Universidade de São Paulo (USP)
dc.description.affiliation Butantan Inst, Immunochem Lab, BR-05503900 São Paulo, SP, Brazil
dc.description.affiliation Butantan Inst, Ctr Toxins Immuneresponse & Cell Signaling CeTICS, BR-05503900 São Paulo, SP, Brazil
dc.description.affiliation Universidade Federal de São Paulo, Dept Biochem, São Paulo, Brazil
dc.description.affiliation Univ São Paulo, Dept Pharmacol, São Paulo, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Dept Biochem, São Paulo, Brazil
dc.description.sponsorshipID CAPES: 63/2010
dc.description.sponsorshipID FAPESP: 2012/06677-0
dc.identifier.doi 10.1016/j.bbagen.2015.02.005
dc.description.source Web of Science
dc.identifier.wos WOS:000353736100009



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