Navegação Eventos - Resumos por Autores IPEN "AFFONSO, REGINA"

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  • IPEN-DOC 24637

    TARGINO, BARBARA ; PINTO, THAIS L. ; SILVA, EVILY F. ; SOMESSARI, E.S.R. ; BELLINI, MARIA H. ; AFFONSO, REGINA . Evaluation of low doses of gamma irradiation in the formation of mineralization nodules in osteoblasts culture. In: ANAIS DA SOCIEDADE BRASILEIRA DE BIOCIENCIAS NUCLEARES, 09-11 de outubro, 2017, São Paulo, SP. Abstract... Rio de Janeiro, RJ: Sociedade Brasileira de Biociências Nucleares, 2017. p. 116-116.

    Abstract: Introduction: Osteoblasts are specialized fibroblasts that secrete and mineralize the bone matrix. The mineralized extracellular matrix is mainly composed of type I collagen, osteocalcin, and the inorganic mineral hydroxylapatite1. The use of radiation as therapy in some cancers causes great bone loss. However, low dose radiation may have the opposite effect. Low dose X-irradiation on osteoblastic culture had effects on proliferation and differentiation with increase of mineralization nodules2. However, there is little information on the potential therapeutic efficacy of low-dose gamma-irradiation in the formation of mineralization nodules. Objective: To evaluate the effects of irradiation with 60Co γ-rays in low doses in the formation of mineralization nodules in culture of osteoblasts. Methods: MC3T3-E1 cells were bought by the Banco de Células do Rio de Janeiro, Brazil (MC3T3-E1 Subclone 14). The cells were cultured in α-MEM medium consisting of 10% FBS and without β-glycerophosphate and L-ascorbic acid (GIBCO, Custom Product, Catalog No. A1049001) (Zhao Y, Guan H, Liu S et al. Biol. Pharm. Bull. 2005, 28(8):1371-1376). Plating efficiency assays: cells were plated at a density of 100 cell/plate into 60 mm Petri dishes. After 14 days the places were stained with violet crystal and the colonies were counted. -glycerophosphate and 50 mg/ml ascorbic acid, and analyzed on days 7, 14 and 21. Osteoblast culture irradiation assay: cells were plated at a density of 1x 105 cells/plate on 60 mm dishes and the next day were irradiated by 60Co source with 0 (as the control), 0.5, 1.0, 1.5 and 2.0 Gy using the GammaCell 220 – Irradiation Unit of Canadian-Atomic Energy Commission Ltd. (CTR-IPEN). On day 21 of culture, undifferentiated (without ascorbic acid and β-glycerophosphate), differentiating cells (0 Gy) and irradiated cells at different doses, the medium was removed, cells were washed with phosphate buffer saline, fixed with 70% ethyl alcohol and stained with Alizarin red S (Sigma). All in three biological replicates (a total of 54 samples) and multiple comparisons were assessed by One-way ANOVA followed by Bonferroni´s tests with GraphPad Prism version 6.0 software. P< 0.05 was considered statistically significant. Results: Plating efficiency (PF) analysis is generally considered to be the gold standard of assays for testing the sensitivity of cell lines to ionizing radiation or other cytotoxic agents in vitro. The results obtained were a PF of 30% for non-irradiated culture, however, the irradiated culture obtained 40% in relation to the no-irradiated one, already with 0.5 Gy, and this percentage was maintained in the other larger doses. Regarding the evaluation of the formation of mineralization nodules, significant difference in 0.5 Gy group was observed compared with the control group (0 Gy), 64.7±1.8 and 53.0±0.9, respectively. The groups of 1.0, 1.5 and 2.0 Gy obtained a decrease in the mineralization nodules. The data obtained with increasing irradiation produced an increase of mineralization nodules up to 0.5 Gy and in the higher doses had a decrease. Applying the data in a non-linear function it is observed that the line has a decreasing tendency with the negative angular coefficient. This analysis is in agreement with the hormesis model, in which low doses induce a stimulatory effect while high doses cause inhibition4. Conclusions: This study is one among the first that investigating the biophysics of low-dose gamma-irradiation on MC3T3-E1 culture, focusing on the potential applications in bone replacement therapy.

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  • IPEN-DOC 24265

    SILVA, FELIPE D. ; SUZUKI, MIRIAM ; OLIVEIRA, JOAO ; FREIRE, RENAN ; BARTOLINI, PAOLO ; SOARES, CARLOS ; AFFONSO, REGINA . Expression of human prolactin in HEK293T using different transfection reagents. In: ANNUAL MEETING OF THE BRAZILIAN SOCIETY FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY, 46th, July 27-30, 2017, Águas de Lindóia, SP. Abstract... São Paulo, SP: Sociedade Brasileira de Bioquímica e Biologia Molecular, 2017.

    Abstract: INTRODUCTION Prolactin is a hormone produced by the pituitary gland with numerous functions, such as lactation, reproduction, osmotic and immune regulation. This hormone is upregulated in cases of lack of lactation, infertility and cancer. Recombinant prolactin has been produced in Escherichia coli with an initial methionine which may cause immunological reactions, or in its authentic form in mammalian cells. Our laboratory has already synthesized human prolactin (hPRL) without initial methionine in E. coli periplasm and Chinese hamster ovary cells. CHO cells have been widely used in the synthesis of human recombinant proteins because of their similarity with human post-translational modifications as glycosylation. The HEK293, a human embryonic kidney cell, can do diverse glycosylation depend on culture conditions. OBJECTIVES This work compares different transfection reagents in the production of hPRL in HEK293T. MATERIALS AND METHODS The hPRL cDNA was inserted into the pEDdc vector donated by the Genetics Institute, USA. Three transfection reagents were used: LipofectamineTM (Thermo), XfectTM (Clontech), and ExpiFectamineTM (Thermo). HEK293T cells, a human strain, were cultured in 10 cm² Ø petri dishes with RPMI 1640 medium with 10% fetal bovine serum (FBS). After transfection, the medium was changed to serum free CHO-S-SFM II (Invitrogen, USA). 100% of the medium was collected and changed every two days. The collected medium was stored at -80°C. Samples were analyzed by SDS-PAGE, Western blotting and HPLC. DISCUSSION AND RESULTS The glycosylated and non-glycosylated hPRL forms secreted into the culture medium were confirmed by Western blot and RPHPLC in the three transfected cultures in recombinant human cells. The reagent with the best result was Xfect (2 μg/mL), followed by Lipofectamine (1.6 μg/mL) and Expifectamine (1.2 μg/mL). CONCLUSION The transient expression of hPRL using HEK293T cells enable laboratory production of glycosylated hPRL for future studies of N-glycans produced by these cells.

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  • IPEN-DOC 28589

    SANTOS, CAROLINA M. dos ; SAMPAIO, SUELEN de B.; SANTANA, FAGNER ; LEITE, RODRIGO C. ; PRATA, BEATRIZ A. ; AFFONSO, REGINA . A new approach for purification of the catalytic site of the Angiotensin Conversion Enzyme, N domain, mediated by the ELP-Inten system. In: CONGRESS OF THE INTERNATIONAL UNION FOR PURE APPLIED BIOPHYSICS, 20th; ANNUAL MEETING OF THE BRAZILIAN SOCIETY FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY, 50th; CONGRESS OF BRAZILIAN BIOPHYSICS SOCIETY, 45th; BRAZILIAN SOCIETY ON NUCLEAR BIOSCIENCES CONGRESS, 13th, October 4-8, 2021, São Paulo, SP. Abstract... São Paulo, SP: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), 2021. p. 143-143.

    Abstract: Angiotensin-converting enzyme I, ACE, is a key part of the renin-angiotensin system whose main function is to regulate blood pressure and balance of salts in the body. ACE1 has two isoforms, somatic, sACE, and testicular, tACE. sACE possesses two domains, N- C-, with catalytic sites which exhibit 60% sequence identity. These domains differ in terms of chloride-ion activation profiles, rates of peptide hydrolysis and sensitivities to various inhibitors. N-domain has specific action in the hydrolyze of Alzheimer’s diseases beta amyloid bodies and angiotensin 1-7, which active the MAS receptor and triggering anti-thrombotic and anti-inflammatory actions. The objective this work was to obtain catalytic site Ala361 to Gli468 of the N-domain region, csACEN, isolation without chromatographic and denaturant chemical process. For that, a new methodology was used in the expression of the csACEN peptide, in which the peptide was linked to the elastin-like polypeptide, ELP, and Intein, and expressed at 37C. The characterization of catalytic site was made by SDS-PAGE and dot blotting. The culture temperature at 37C significantly increased the expression of the ELP/Intein/csACEN fusion protein. This culture was lysed at a low temperature allowing the fusion protein to become soluble. The precipitation of ELP at high concentrations of ammonium sulfate were obtained in 0.57 M and 0.8 M. Intein autocleavage occurs at acidic pH and it is important to pay attention to: pI 6.65 for csACEN and pI 6.87 for ELPcsACEN, which are very low. The best autocleavage efficiency was with MES and TriHCl buffers, pH 6.3 and 6.8, respectively, in which pure csACEn peptide was obtained. The strategy used to obtain the Ala361 to Gli468 catalytic site in soluble and pure form was obtained with success and the protocol for obtaining similar peptides was established.

    Palavras-Chave: angiotensin; enzymes; inflammation; thrombosis; temperature dependence

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  • IPEN-DOC 25985

    SANTOS, CAROLINA M. dos ; FIGUEIREDO, ALINE M. de ; LEITE, RODRIGO C. ; CAMARGO, NATANE M. de ; AFFONSO, REGINA . A new approach to obtain the catalytic site of human Angiotensin Converting Enzyme. In: EUROPEAN SYMPOSIUM ON BIOCHEMICAL ENGINEERING SCIENCES, 12th, September 9-12, 2018, Lisbon, Portugal. Abstract... Frankfurt am Main, Germany: European Society of Biochemical Engineering Sciences - ESBES, 2018.

    Abstract: Angiotensin-converting enzyme I (ACE) is a key part of the renin-angiotensin system whose main function is to regulate blood pressure. The sACE possesses two domains, N- C-, with catalytic sites which exhibit 60% sequence identity. These domains differ in terms of chloride-ion activation profiles, rates of peptide hydrolysis of angiotensin I, bradykinin, angiotensina (1-7), beta-amyloid peptide and sensitivities to various inhibitors. A more detailed analysis shows that these regions are composed of HEMGH and EAIGD sequences, which are the catalytic sites. Our question is: If the synthesis of catalytic sites with corrects structure and activity could be a good model per si to study new drugs. In our laboratory the catalytic site of the C-domain was obtained with correct structural conformation and with enzymatic activity. The objective this work is to obtain the Ala361 to Gli468 catalytic site, N-domain, in a structural conformation that resembles its native form. The 380 pb cDNA to catalytic site was cloned in the pE1 vector (kindly provided by Dr. David Wood), elastinlike-polyptide (ELP) tag sequence was linked with catalytic site, ELP~csACEn recombinant protein, this was expressed in bacteria with Terrificus broth with 0.1 mM IPTG for 20h. Harvested cells were resuspended in TE buffer, after sonication and centrifugation the pellet was resuspended the same buffer. The ELP~csACEn was precipitated with 0.8 M ammonium sulfate and the tag sequence was cleaved by pH change, pH 6.2. All steps were analyzed by SDS-PAGE, Dot and Western blotting. The catalytic site was synthesized from bacterial system with ELP sequence tag in soluble form. The purification process was done by ammonium sulfate precipitation and cleavage of the ELP sequence by changing to acidic pH. The characterization of catalytic site by SDS-PAGE shows that this is pure and Western blotting immunological assay confirmed the identity of the protein as csACEn. The strategy used to obtain the Ala361 to Gli468 catalytic site in soluble and pure form was successful. The next steps: we will continue with the Maldi-tof and structural conformation analyzes.

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  • IPEN-DOC 29545

    PRATA, BEATRIZ A. ; SANTOS, CAROLINA M. dos ; AFFONSO, REGINA . Optimization of the process of expression in E. coli and purification of the catalytic sites of the ACE1 by the ELP-Intein system. In: ANNUAL MEETING OF THE BRAZILIAN SOCIETY FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY (SBBq), 51st; CONGRESS OF BRAZILIAN BIOPHYSICAL SOCIETY (SBBf)/LATIN AMERICAN FEDERATION OF BIOPHYSICAL SOCIETIES (Lafebs), 46th, September 5-8, 2022, Águas de Lindóia, SP. Abstract... São Paulo, SP: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2022. p. 220-220.

    Abstract: INTRODUCTION: Angiotensin I-converting enzyme (ACE) is a fundamental part of the renin-angiotensin system; this has two domains, N- and C-, each of which has a catalytic site that exhibits 60% sequence identity. Its actions are in the control of blood pressure, protection of the brain by cleavage of beta-amyloid bodies, cell proliferation, formation of hematopoietic stem cells, among others. OBJECTIVES: Obtaining the catalytic sites Ala361 to Gly468 (N domain region, csACEN) and Ala959 to Ser1066 (C domain region, csACEC) in pure form and with their correct structural conformation. MATERIALS AND METHODS: Expression conditions of pE1csACEN and pE1csACEC vectors in E. coli BL21(DE3) strain: cultures grown in Terrific Broth at 37⁰C at 140 rpm for 20–24 h and 0.1 mM IPTG. Purification by Elastin-like Polypeptide (ELP) precipitation: ELP-bound catalytic sites were purified with two ammonium sulfate precipitations (ASp). Remotion of ELP: by autocleavage of the Intein sequence using the buffers: sodium phosphate, sodium cacodylate, MES and Tris-HCl. The ELP/Intein was removed from the sample by ASp. The analyzes of all stages of the process were performed by SDS-PAGE and Dot blotting. DISCUSSION AND RESULTS: The differential for obtaining the pure peptides was the temperature of 37⁰C, with a significant increase in expression concerning the cultivation of 16⁰C. In the ELP purification steps, ammonium sulfate buffer concentrations of 0.57 M and 0.8 M were the most efficient. Intein's self-cleaving was more efficient with MES buffers and Tris-HCl for ELPsACEN and ELPsACEC, respectively. Structural analysis by Circular Dichroism and Fluorescence confirmed the correct structure of the pure peptides. CONCLUSION: In the present work, we defined the most efficient conditions for expression, purification, and obtaining of ACE catalytic sites in pure form. The csACEN and csACEC peptides will allow greater assertiveness in obtaining and characterizing new hypertensive drugs and in the hydrolysis of substrates such as beta-amyloid.

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  • IPEN-DOC 29548

    KOTANI, PALOMA O. ; FERRO, DAPHNE M. ; TAVARES, LAURA P. ; AFFONSO, REGINA ; ORTIZ, NILCE . Using TiO2-Diatomite for photodisinfection in contaminated wastewater. In: ANNUAL MEETING OF THE BRAZILIAN SOCIETY FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY (SBBq), 51st; CONGRESS OF BRAZILIAN BIOPHYSICAL SOCIETY (SBBf)/LATIN AMERICAN FEDERATION OF BIOPHYSICAL SOCIETIES (Lafebs), 46th, September 5-8, 2022, Águas de Lindóia, SP. Abstract... São Paulo, SP: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2022. p. 212-212.

    Abstract: INTRODUCTION: The urban pressure reduced water availability and quality through the years, promoting the development of water treatment and disinfection processes such as the Advanced Oxidation Process (AOP). A highly efficient catalyst with Diatomite as biotemplate and solar energy can enhance hydroxyl radicals (OH) production for disinfection and pollutants degradation. Preliminary TiO2-Diatomite experiments with Escherichia coli provided valuable insights on its photodisinfection efficiency, legitimating its usage in the wastewater samples presented in this study. OBJECTIVES: Evaluate the use of TiO2-Diatomite in photodisinfection process in contaminated wastewater. MATERIALS AND METHODS: TiO2 synthesis used titanium isopropoxide sol-gel process with Diatomite powder, the filtration step followed the mixed water suspension, and the drying process lasted overnight. The wastewater samples were collected from a household washing machine and 0.05 g of TiO2-Diatomite were added in the photodisinfection reactor. The total reaction lasted for 90 minutes in the solar chamber with all parameters controlled. The suspension aliquots were collected after 30 minutes of agitation and plated on LB agar at Petri plates. After incubation, the emerged colonies were counted through software (OpenCFU) and the data processed using R programming language. DISCUSSION AND RESULTS: The Scanning Electron Microscopy (SEM) micrograph of TiO2-Diatomite presented enhanced surface area and microstructure obtained by biotemplate addition. The bacterial inactivation percentage was above 75 % for 1 hour of solar radiation exposure. Kinetics models indicated better correspondence with interparticle reaction. CONCLUSION: Photodisinfection kinetics studies provided more efficient bacterial inactivation with the addition of 0.05 g of TiO2-Diatomite in the sample. The study presents an affordable and sustainable treatment using a viable renewable energy source for application in distant areas with contaminated effluents with the addition of a reagent easily obtained by government agencies.

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O gerenciamento do Repositório está a cargo da Biblioteca do IPEN. Constam neste RI, até o presente momento 20.950 itens que tanto podem ser artigos de periódicos ou de eventos nacionais e internacionais, dissertações e teses, livros, capítulo de livros e relatórios técnicos. Para participar do RI-IPEN é necessário que pelo menos um dos autores tenha vínculo acadêmico ou funcional com o Instituto. Nesta primeira etapa de funcionamento do RI, a coleta das publicações é realizada periodicamente pela equipe da Biblioteca do IPEN, extraindo os dados das bases internacionais tais como a Web of Science, Scopus, INIS, SciElo além de verificar o Currículo Lattes. O RI-IPEN apresenta também um aspecto inovador no seu funcionamento. Por meio de metadados específicos ele está vinculado ao sistema de gerenciamento das atividades do Plano Diretor anual do IPEN (SIGEPI). Com o objetivo de fornecer dados numéricos para a elaboração dos indicadores da Produção Cientifica Institucional, disponibiliza uma tabela estatística registrando em tempo real a inserção de novos itens. Foi criado um metadado que contém um número único para cada integrante da comunidade científica do IPEN. Esse metadado se transformou em um filtro que ao ser acionado apresenta todos os trabalhos de um determinado autor independente das variáveis na forma de citação do seu nome.

A elaboração do projeto do RI do IPEN foi iniciado em novembro de 2013, colocado em operação interna em julho de 2014 e disponibilizado na Internet em junho de 2015. Utiliza o software livre Dspace, desenvolvido pelo Massachusetts Institute of Technology (MIT). Para descrição dos metadados adota o padrão Dublin Core. É compatível com o Protocolo de Arquivos Abertos (OAI) permitindo interoperabilidade com repositórios de âmbito nacional e internacional.

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O Repositório Digital do IPEN é um equipamento institucional de acesso aberto, criado com o objetivo de reunir, preservar, disponibilizar e conferir maior visibilidade à Produção Científica publicada pelo Instituto, desde sua criação em 1956.

Operando, inicialmente como uma base de dados referencial o Repositório foi disponibilizado na atual plataforma, em junho de 2015. No Repositório está disponível o acesso ao conteúdo digital de artigos de periódicos, eventos, nacionais e internacionais, livros, capítulos, dissertações, teses e relatórios técnicos.

A elaboração do projeto do RI do IPEN foi iniciado em novembro de 2013, colocado em operação interna em julho de 2014 e disponibilizado na Internet em junho de 2015. Utiliza o software livre Dspace, desenvolvido pelo Massachusetts Institute of Technology (MIT). Para descrição dos metadados adota o padrão Dublin Core. É compatível com o Protocolo de Arquivos Abertos (OAI) permitindo interoperabilidade com repositórios de âmbito nacional e internacional.

O gerenciamento do Repositório está a cargo da Biblioteca do IPEN. Constam neste RI, até o presente momento 20.950 itens que tanto podem ser artigos de periódicos ou de eventos nacionais e internacionais, dissertações e teses, livros, capítulo de livros e relatórios técnicos. Para participar do RI-IPEN é necessário que pelo menos um dos autores tenha vínculo acadêmico ou funcional com o Instituto. Nesta primeira etapa de funcionamento do RI, a coleta das publicações é realizada periodicamente pela equipe da Biblioteca do IPEN, extraindo os dados das bases internacionais tais como a Web of Science, Scopus, INIS, SciElo além de verificar o Currículo Lattes. O RI-IPEN apresenta também um aspecto inovador no seu funcionamento. Por meio de metadados específicos ele está vinculado ao sistema de gerenciamento das atividades do Plano Diretor anual do IPEN (SIGEPI). Com o objetivo de fornecer dados numéricos para a elaboração dos indicadores da Produção Cientifica Institucional, disponibiliza uma tabela estatística registrando em tempo real a inserção de novos itens. Foi criado um metadado que contém um número único para cada integrante da comunidade científica do IPEN. Esse metadado se transformou em um filtro que ao ser acionado apresenta todos os trabalhos de um determinado autor independente das variáveis na forma de citação do seu nome.