PATRICK JACK SPENCER

Resumo

Possui graduação em Ciências Biológicas pela Universidade Presbiteriana Mackenzie (1991), mestrado em Tecnologia Nuclear pela Universidade de São Paulo (1995) e doutorado em Tecnologia Nuclear pela Universidade de São Paulo (2000) tendo sido bolsista sandwich no US Army Medical Research Institute for Infeccious Diseases (98-99). É responsável pelo Biotério de criação e manutenção de animais de laboratório do IPEN. Tem experiência na área de Bioquímica, com ênfase em Proteínas, atuando principalmente nos seguintes temas: veneno, proteínas, bothrops, irradiação e miotoxina.(Texto extraído do Currículo Lattes em 22 dez. 2021)

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Agora exibindo 1 - 3 de 3
  • Artigo IPEN-doc 23046
    Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros
    2017 - FUCASE, TAMARA M.; SCIANI, JULIANA M.; CAVALCANTE, INGRID; VIALA, VINCENT L.; CHAGAS, BRUNO B.; PIMENTA, DANIEL C.; SPENCER, PATRICK J.
    Background: Venoms represent a still underexplored reservoir of bioactive components that might mitigate or cure diseases in conditions in which conventional therapy is ineffective. The bradykinin-potentiating peptides (BPPs) comprise a class of angiotensin-I converting enzyme (ACE) inhibitors. The BPPs usually consist of oligopeptides with 5 to 13 residues with a high number of proline residues and the tripeptide Ile-Pro-Pro (IPP-tripeptide) in the C-terminus region and have a conserved N-terminal pyroglutamate residue. As a whole, the action of the BPPs on prey and snakebite victims results in the decrease of the blood pressure. The aim of this work was to isolate and characterize novel BPPs from the venom of Bitis gabonica rhinoceros. Methods: The crude venom of B. g. rhinoceros was fractionated by size exclusion chromatography and the peptide fraction (<7 kDa) was separated by reverse phase chromatography (RP-HPLC) and analyzed by ESI-IT-TOF-MS/MS. One new BPP was identified, synthetized and assayed for ACE inhibition and, in vivo, for edema potentiation. Results: Typical BPP signatures were identified in three RP-HPLC fractions. CID fragmentation presented the usual y-ion of the terminal P-P fragment as a predominant signal at m/z 213.1. De novo peptide sequencing identified one Bothrops-like BPP and one new BPP sequence. The new BPP was synthesized and showed poor inhibition over ACE, but displayed significant bradykinin-induced edema potentiation. Conclusions: So far, few BPPs are described in Viperinae, and based on the sequenced peptides, two non-canonical sequences were detected. The possible clinical role of this new peptides remains unclear.
  • Artigo IPEN-doc 21327
    Venomics of the Australian eastern brown snake (Pseudonaja textilis): Detection of new venom proteins and splicing variants
    2015 - VIALA, VINCENT L.; HILDEBRAND, DIANA; TRUSCH, MARIA; FUCASE, TAMARA M.; SCIANI, JULIANA M.; PIMENTA, DANIEL C.; ARNI, RAGHUVIR K.; SCHLUTER, HARTMUT; BETZEL, CHRISTIAN; MIRTSCHIM, PETER; DUNSTAN, NATHAN; SPENCER, PATRICK J.
  • Artigo IPEN-doc 21288
    Proteomic analysis of the rare Uracoan rattlesnake Crotalus vegrandis venom: Evidence of a broad arsenal of toxins
    2015 - VIALA, VINCENT L.; HILDEBRAND, DIANA; FUCASE, TAMARA M.; SCIANI, JULIANA M.; PREZOTTO NETO, JOSE P.; RIEDNER, MARIA; SANCHES, LEONARDO; NISHIMURA, PAULA J.; OGUIURA, NANCY; PIMENTA, DANIEL C.; SCHLUTER, HARTMUT; BETZEL, CHRISTIAN; ARNI, RAGHUVIR K.; SPENCER, PATRICK J.