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Insights into cardiovascular effects of proline-rich oligopeptide (Bj-PRO-10c) revealed by structure–activity analyses: dissociation of antihypertensive and bradycardic effects (2014)

  • Authors:
  • USP affiliated authors: SCHREIER, SHIRLEY - IQ ; CAMARGO, ANTONIO CARLOS MARTINS DE - ICB
  • USP Schools: IQ; ICB
  • DOI: 10.1007/s00726-013-1630-x
  • Subjects: PRESSÃO SANGUÍNEA; OLIGOPEPTÍDEOS
  • Language: Inglês
  • Imprenta:
  • Source:
    • Título do periódico: Amino Acids
    • ISSN: 0939-4451
    • Volume/Número/Paginação/Ano: v. 46, n. 2, p. 401-413: +, 2014
  • Acesso online ao documento

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    Informações sobre o DOI: 10.1007/s00726-013-1630-x (Fonte: oaDOI API)
    • Este periódico é de assinatura
    • Este artigo NÃO é de acesso aberto
    • Cor do Acesso Aberto: closed
    Versões disponíveis em Acesso Aberto do: 10.1007/s00726-013-1630-x (Fonte: Unpaywall API)

    Título do periódico: Amino Acids

    ISSN: 0939-4451,1438-2199



      Não possui versão em Acesso aberto
    Informações sobre o Citescore
  • Título: Amino Acids

    ISSN: 0939-4451

    Citescore - 2017: 2.94

    SJR - 2017: 1.135

    SNIP - 2017: 0.989


  • How to cite
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    • ABNT

      PASCHOAL, Juliana F. B; MIRANDA , José R. R; CARRETERO, Gustavo Penteado Battesine; et al. Insights into cardiovascular effects of proline-rich oligopeptide (Bj-PRO-10c) revealed by structure–activity analyses: dissociation of antihypertensive and bradycardic effects. Amino Acids, New York, v. 46, n. 2, p. 401-413: +, 2014. Disponível em: < http://dx.doi.org/10.1007/s00726-013-1630-x > DOI: 10.1007/s00726-013-1630-x.
    • APA

      Paschoal, J. F. B., Miranda , J. R. R., Carretero, G. P. B., Melo, R. L. de, Santos, R. A. S. dos, Carlos H. Xavier,, et al. (2014). Insights into cardiovascular effects of proline-rich oligopeptide (Bj-PRO-10c) revealed by structure–activity analyses: dissociation of antihypertensive and bradycardic effects. Amino Acids, 46( 2), 401-413: +. doi:10.1007/s00726-013-1630-x
    • NLM

      Paschoal JFB, Miranda JRR, Carretero GPB, Melo RL de, Santos RAS dos, Carlos H. Xavier, Schreier S, Camargo ACM de, Ianzer D. Insights into cardiovascular effects of proline-rich oligopeptide (Bj-PRO-10c) revealed by structure–activity analyses: dissociation of antihypertensive and bradycardic effects [Internet]. Amino Acids. 2014 ; 46( 2): 401-413: +.Available from: http://dx.doi.org/10.1007/s00726-013-1630-x
    • Vancouver

      Paschoal JFB, Miranda JRR, Carretero GPB, Melo RL de, Santos RAS dos, Carlos H. Xavier, Schreier S, Camargo ACM de, Ianzer D. Insights into cardiovascular effects of proline-rich oligopeptide (Bj-PRO-10c) revealed by structure–activity analyses: dissociation of antihypertensive and bradycardic effects [Internet]. Amino Acids. 2014 ; 46( 2): 401-413: +.Available from: http://dx.doi.org/10.1007/s00726-013-1630-x

    Referências citadas na obra
    Alana I, Parker JC, Gault VA, Flatt PR, O’Harte FP, Malthouse JP, Hewage CM (2006) NMR and alanine scan studies of glucose-dependent insulinotropic polypeptide in water. J Biol Chem 281(24):16370–16376
    Biedermannova L, ER K, Berka K, Hobza P, Vondrasek J (2008) Another role of proline: stabilization interactions in proteins and protein complexes concerning proline and tryptophane. Phys Chem Chem Phys 10(42):6350–6359
    Bunag RD, Walaszek EJ, Mueting N (1975) Sex differences in reflex tachycardia induced by hypotensive drugs in unanesthetized rats. Am J Physiol 229(3):652–656
    Camargo AC, Fernandes BL, Cruz L, Ferro ES (2012a) Bioactive peptides produced by limited proteolysis. Morgan & Claypool publishers. doi: 10.4199/C00056ED1V01Y201204NPE002
    Camargo AC, Ianzer D, Guerreiro JR, Serrano SM (2012b) Bradykinin-potentiating peptides: beyond captopril. Toxicon 59(4):516–523
    Carmona AK, Juliano L (1996) Inhibition of angiotensin converting enzyme and potentiation of bradykinin by retro-inverso analogues of short peptides and sequences related to angiotensin I and bradykinin. Biochem Pharmacol 51(8):1051–1060
    Corzo G, Sabo JK, Bosmans F, Billen B, Villegas E, Tytgat J, Norton RS (2007) Solution structure and alanine scan of a spider toxin that affects the activation of mammalian voltage-gated sodium channels. J Biol Chem 282(7):4643–4652
    Cunningham BC, Wells JA (1989) High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science 244(4908):1081–1085
    Cushman DW, Pluscec J, Williams NJ, Weaver ER, Sabo EF, Kocy O, Cheung HS, Ondetti MA (1973) Inhibition of angiotensin-coverting enzyme by analogs of peptides from Bothrops jararaca venom. Experientia 29(8):1032–1035
    De Sousa FB, Denadai AML, Lula IS, Ianzer D, Malaspina ER, Camargo ACM, Santos RAS, Sinisterra RD (2010) Structural and physical–chemical evaluation of bradykinin potentiating peptide and its high soluble supramolecular complex. J Incl Phenom Macrocycl Chem 67:407–422
    Flam BR, Hartmann PJ, Harrell-Booth M, Solomonson LP, Eichler DC (2001) Caveolar localization of arginine regeneration enzymes, argininosuccinate synthase, and lyase, with endothelial nitric oxide synthase. Nitric Oxide 5(2):187–197
    Goldberg M, Gomez-Orellana I (2003) Challenges for the oral delivery of macromolecules. Nat Rev Drug Discov 2(4):289–295
    Guerreiro JR, Lameu C, Oliveira EF, Klitzke CF, Melo RL, Linares E, Augusto O, Fox JW, Lebrun I, Serrano SM, Camargo AC (2009) Argininosuccinate synthetase is a functional target for a snake venom anti-hypertensive peptide: role in arginine and nitric oxide production. J Biol Chem 284(30):20022–20033
    Gund P (1977) Three-dimensional pharmacophoric pattern searching. In: progress in molecular and subcellular biology, vol 5. pp 117–143
    Hayashi MA, Murbach AF, Ianzer D, Portaro FC, Prezoto BC, Fernandes BL, Silveira PF, Silva CA, Pires RS, Britto LR, Dive V, Camargo AC (2003) The C-type natriuretic peptide precursor of snake brain contains highly specific inhibitors of the angiotensin-converting enzyme. J Neurochem 85(4):969–977
    Ianzer D, Konno K, Marques-Porto R, Vieira Portaro FC, Stocklin R, Martins de Camargo AC, Pimenta DC (2004) Identification of five new bradykinin potentiating peptides (BPPs) from Bothrops jararaca crude venom by using electrospray ionization tandem mass spectrometry after a two-step liquid chromatography. Peptides 25(7):1085–1092
    Ianzer D, Santos RA, Etelvino GM, Xavier CH, de Almeida, Santos J, Mendes EP, Machado LT, Prezoto BC, Dive V, de Camargo AC (2007) Do the cardiovascular effects of angiotensin-converting enzyme (ACE) I involve ACE-independent mechanisms? new insights from proline-rich peptides of Bothrops jararaca. J Pharmacol Exp Ther 322(2):795–805
    Ianzer DA, Bernardes I, Lima AM, Santos RAS, Xavier CH, Fontes MAP (2010) BPP-10c from Bothrops jararaca venom changes behavioral and cardiovascular responses to acute stress exposure. FASEB J 24(811):814
    Ianzer D, Xavier CH, Fraga FC, Lautner RQ, Guerreiro JR, Machado LT, Mendes EP, de Camargo AC, Santos RA (2011) BPP-5a produces a potent and long-lasting NO-dependent antihypertensive effect. Ther Adv Cardiovasc Dis 5(6):281–295
    Isaac RE, Bland ND, Shirras AD (2009) Neuropeptidases and the metabolic inactivation of insect neuropeptides. Gen Comp Endocrinol 162(1):8–17
    Kelly MA, Chellgren BW, Rucker AL, Troutman JM, Fried MG, Miller AF, Creamer TP (2001) Host-guest study of left-handed polyproline II helix formation. Biochemistry 40(48):14376–14383
    Lee HJ, Zheng JJ (2010) PDZ domains and their binding partners: structure, specificity, and modification. Cell Commun Signal 8:8. doi: 10.1186/1478-811X-8-8
    Machado RS, Guest JR, Williamson MP (1993) Mobility in pyruvate dehydrogenase complexes with multiple lipoyl domains. FEBS Lett 323(3):243–246
    Marlborough DI, Fisher GH, Ryan JW (1981) Circular dichroism spectra of some lower homologs of bradykinin potentiating peptide 9 alpha. Arch Biochem Biophys 210(1):43–48
    Meng HY, Thomas KM, Lee AE, Zondlo NJ (2006) Effects of i and i + 3 residue identity on cis-trans isomerism of the aromatic(i + 1)-prolyl(i + 2) amide bond: implications for type VI beta-turn formation. Biopolymers 84(2):192–204
    Moradi M, Babin V, Roland C, Sagui C (2010) A classical molecular dynamics investigation of the free energy and structure of short polyproline conformers. J Chem Phys 133(12):125104
    Murayama N, Hayashi MA, Ohi H, Ferreira LA, Hermann VV, Saito H, Fujita Y, Higuchi S, Fernandes BL, Yamane T, de Camargo AC (1997) Cloning and sequence analysis of a Bothrops jararaca cDNA encoding a precursor of seven bradykinin-potentiating peptides and a C-type natriuretic peptide. Proc Natl Acad Sci USA 94(4):1189–1193
    Neduva V, Russell RB (2006) Peptides mediating interaction networks: new leads at last. Curr Opin Biotechnol 17(5):465–471
    Quartara L, Ricci R, Meini S, Patacchini R, Giolitti A, Amadesi S, Rizzi C, Rizzi A, Varani K, Borea PA, Maggi CA, Regoli D (2000) Ala scan analogues of HOE 140. Synthesis and biological activities. Eur J Med Chem 35(11):1001–1010
    Rucker AL, Pager CT, Campbell MN, Qualls JE, Creamer TP (2003) Host-guest scale of left-handed polyproline II helix formation. Proteins 53(1):68–75
    Shen LJ, Beloussow K, Shen WC (2005) Accessibility of endothelial and inducible nitric oxide synthase to the intracellular citrulline–arginine regeneration pathway. Biochem Pharmacol 69(1):97–104
    Silva CA, Ianzer DA, Portaro FC, Konno K, Faria M, Fernandes BL, Camargo AC (2008a) Characterization of urinary metabolites from four synthetic bradykinin potentiating peptides (BPPs) in mice. Toxicon 52(3):501–507
    Silva CA, Portaro FC, Fernandes BL, Ianzer DA, Guerreiro JR, Gomes CL, Konno K, Serrano SM, Nascimento N, Camargo AC (2008b) Tissue distribution in mice of BPP 10c, a potent proline-rich anti-hypertensive peptide of Bothrops jararaca. Toxicon 51(4):515–523
    Thomas KM, Naduthambi D, Zondlo NJ (2006) Electronic control of amide cis–trans isomerism via the aromatic-prolyl interaction. J Am Chem Soc 128(7):2216–2217
    Uekama K, Hirayama F, Irie T (1998) Cyclodextrin drug carrier systems. Chem Rev 98(5):2045–2076
    Zelanis A, Tashima AK, Rocha MM, Furtado MF, Camargo AC, Ho PL, Serrano SM (2010) Analysis of the ontogenetic variation in the venom proteome/peptidome of Bothrops jararaca reveals different strategies to deal with prey. J Proteome Res 9(5):2278–2291