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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Artigo IPEN-doc 29496 Action of bromelain and ficin on horse anti Bothrops sp venom antibodies2022 - MARQUES, RODOLFO F.; QUINTILIO, WAGNER; KNIRSCH, MARCOS C.; FUCASE, TAMARA M.; SPENCER, PATRICK J.; STEPHANO, MARCO A.The treatment with hyperimmune sera constitute the only specific and effective therapy available against snakebite envenomation, most common in developing countries. Serum quality is an important factor on patient recovery time and in the incidence of death and permanent disability. To date, most sera consist of pepsin digested IgG antibodies harvested from hyperimmune animals. The use of animal derived enzymes, such as pepsin, to digest IgG, constitute a source of adventitious agents and contaminants, such as porcine circovirus. The present study aims to evaluate the use of the plant derived enzymes bromelain and ficin, as an alternative to pepsin. To this purpose, horse serum immunized against Bothrops venoms was purified with caprylic acid and digested with bromelain or ficin. SDS-PAGE results evidence the formation of F(ab)’2 fragments and suggest that a digestion time superior to 8 hours may be required to completely digest the antibodies with bromelain or ficin. F(ab)’2 fragments obtained by digestion with either bromelain or ficin digestion preserved the ability to recognize Bothrops sp. venom in western blotting assays. Therefore, both enzymes are suitable for use in large-scale production, minimizing contamination risks and increasing safety and efficiency of serotherapy treatments.Artigo IPEN-doc 27113 Molecular model of cytotoxin-1 from Naja mossambica mossambica venom in complex with chymotrypsin2015 - MUNAWAR, AISHA; AKREM, AHMED; HUSSAIN, ASHIQ; SPENCER, PATRICK; BETZEL, CHRISTIANSnake venom is a myriad of biologically active proteins and peptides. Three finger toxins are highly conserved in their molecular structure, but interestingly possess diverse biological functions. During the course of evolution the introduction of subtle mutations in loop regions and slight variations in the three dimensional structure, has resulted in their functional versatility. Cytotoxin-1 (UniProt ID: P01467), isolated from Naja mossambica mossambica, showed the potential to inhibit chymotrypsin and the chymotryptic activity of the 20S proteasome. In the present work we describe a molecular model of cytotoxin- 1 in complex with chymotrypsin, prepared by the online server ClusPro. Analysis of the molecular model shows that Cytotoxin-1 (P01467) binds to chymotrypsin through its loop I located near the N-terminus. The concave side of loop I of the toxin fits well in the substrate binding pocket of the protease. We propose Phe10 as the dedicated P1 site of the ligand. Being a potent inhibitor of the 20S proteasome, cytotoxin-1 (P01467) can serve as a potential antitumor agent. Already snake venom cytotoxins have been investigated for their ability as an anticancer agent. The molecular model of cytotoxin-1 in complex with chymotrypsin provides important information towards understanding the complex formation.Artigo IPEN-doc 20886 New insights into the structural characteristics of irradiated crotamine2015 - OLIVEIRA, KARINA C.; SPENCER, PATRICK J.; FERREIRA JUNIOR, RUI S.; NASCIMENTO, NANCIArtigo IPEN-doc 20245 Crystallization and preliminary X-ray diffraction studies of an L-amino-acid oxidase from Lachesis multa venom2014 - ULLAH, ANWAR; MASOOD, REHANA; SPENCER, PATRICK J.; MURAKAMI, MARIO T.; ARNI, RAGHUVIR K.Resumo IPEN-doc 13117 The lesson from snake venom: ion transport and glycolysis are couple through the pumping rate of the Na/KAT pase2007 - LIMA, V.M.F. de; HANKE, W.; CAMILLO, M.A.; SPENCER, P.; NASCIMENTO, N.Artigo IPEN-doc 11694 Paralyzing and myotoxic effects of a recombinat bothoropstoxin-I (BthTX-I) on mouse neuromuscular preparations2006 - GALLACCI, MARCIA; OLIVEIRA, MARISTELA; PAI SILVA, MAELI D.; CAVALCANTE, WALTER L.G.; SPENCER, PATRICK J.Artigo IPEN-doc 11621 Study of gamma-radiation effects on crotamine and crotoxin2006 - CASARE, M.S.; SPENCER, P.; CAMPOS, L.A.; NASCIMENTO, N.Artigo IPEN-doc 14835 Structure alteration and immunological properties of sup(60)Co-gamma-rays irradiated bothropstoxin-I2010 - BAPTISTA, J.A.; VIEIRA, D.P.; GALISTEO JUNIOR, A.J.; HIGA, O.Z.; CASARE, M.; YONAMINE, C.M.; CAPRONI, P.; CAMPOS, L.A.; ANDRADE JUNIOR, H.F. de; SPENCER, P.J.; NASCIMENTO, N.Artigo IPEN-doc 18331 Purification, crystallization and preliminary X-ray diffraction analysis of crotamine, a myotoxic polypeptide from the Brazilian snake Crotalus durissus terrificus2012 - CORONADO, MONIKA A.; GEORGIEVA, DESSISLAVA; BUCK, FRIEDRICH; GABDOULKHAKOV, AZAT H.; ULLAH, ANWAR; SPENCER, PATRICK J.; ARNI, RAGHUVIR K.; BETZEL, CHRISTIAN