Development of a Superconductor Multichannel Biogradiometer with SQUIDs DC for use in FoetalMagnetocardiography. Dissertation(Master)

Neste projeto trabalhou-se no desenvolvimento de uma nova instrumentação para registrar medidas de campos magnéticos de origem biológica baseados em sensores SQUID e sistemas auxiliares, com o objetivo de usar este arranjo na aquisição de medidas de magnetocardiografia fetal (MCGf), que consiste no registro dos campos magnéticos gerados pela atividade cardíaca fetal, refletindo seus processos eletrofisiológicos. Esta técnica biomagnética além de ser bastante precisa para obter medidas de campo magnético originado do coração fetal, que é da ordem de dez picoteslas a poucos centímetros de distância do abdômen materno, também realiza medidas de forma não-invasiva, o que a torna bastante promissora. Contudo, não se conseguiu a sensibilidade desejada do sistema biogradiométrico, sendo alcançada uma sensibilidade capaz de detectar o sinal magneto-cardiográfico (MCG) de um sistema cardíaco desenvolvido, que é da ordem de 100 pT. Neste trabalho reuniu-se, ainda, toda a informação obtida pelo grupo de biomagnetismo no decorrer dos últimos anos referente ao sistema biogradiométrico multicanal.In this project we worked in the developing of a new instrumentation for mea- sure magnetic fields of biological source based in SQUID sensors and auxiliares systems, with aim of use this suite in measures of fetal magnetocardiography (fMCG), that is the recording of the magnetic fields generated by the fetal heart's activity, reflecting the electrophysiological processes that happen in it. This biomagnetic technique besides to be accurate enough to obtain measures of the magnetic field originated from the fetal heart, that is of the order of ten picoteslas at a few centimeters distance from the maternal abdomen, also realizes measures in outside sections at the mother's body turning it so promise. However, not obtained the desired sensitivity of the biogradiometer system, achieving just a sensitivity capable of detecting the magnetocardiography (MCG) signal of a developed cardiac system, which is about 100 pT. This work has met, yet, all information obtained by the biomagnetism group over the past years referent to the multichannel biogradiometer system

Interaction between nanoparticles, membranes and proteins: A surface plasmon resonance study

International audienceRegardless of the promising use of nanoparticles (NPs) in biomedical applications, several toxic effects have increased the concerns about the safety of these nanomaterials. Although the pathways for NPs toxicity are diverse and dependent upon many parameters such as the nature of the nanoparticle and the biochemical environment, numerous studies have provided evidence that direct contact between NPs and biomolecules or cell membranes leads to cell inactivation or damage and may be a primary mechanism for cytotoxicity. In such a context, this work was focused on the development of a fast and accurate method to characterize the interaction between NPs, proteins and lipidic membranes by surface plasmon resonance imaging (SPRi) technique. The interaction of gold NPs with mimetic membranes was evaluated by monitoring the variation of reflectivity after several consecutive gold NPs injections on the lipidic membranes prepared on the SPRi biochip. The interaction on the membranes with varied lipidic composition was compared regarding the total surface concentration density of gold NPs adsorbed on them. Then, the interaction of gold and silver NPs with blood proteins was analyzed regarding their kinetic profile of the association/dissociation and dissociation constants (koff). The surface concentration density on membrane composed of 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine and cholesterol (POPC/cholesterol) was 2.5 times higher than the value found after the injections of gold NPs on POPC only or with dimethyldioctadecylammonium (POPC/DDAB). Regarding the proteins, gold 26 NPs showed a preferential binding to fibrinogen resulting in a value of variation of reflectivity 8 27 times higher than the value found for the other proteins. Differently, silver NPs showed similar 28 interaction on all the tested proteins but with a variation of reflectivity on immunoglobulin G (IgG) 29 2 times higher than the value found for the other tested proteins

Interaction between Nanoparticles, Membranes and Proteins: A Surface Plasmon Resonance Study

Regardless of the promising use of nanoparticles (NPs) in biomedical applications, several toxic effects have increased the concerns about the safety of these nanomaterials. Although the pathways for NPs toxicity are diverse and dependent upon many parameters such as the nature of the nanoparticle and the biochemical environment, numerous studies have provided evidence that direct contact between NPs and biomolecules or cell membranes leads to cell inactivation or damage and may be a primary mechanism for cytotoxicity. In such a context, this work focused on developing a fast and accurate method to characterize the interaction between NPs, proteins and lipidic membranes by surface plasmon resonance imaging (SPRi) technique. The interaction of gold NPs with mimetic membranes was evaluated by monitoring the variation of reflectivity after several consecutive gold NPs injections on the lipidic membranes prepared on the SPRi biochip. The interaction on the membranes with varied lipidic composition was compared regarding the total surface concentration density of gold NPs adsorbed on them. Then, the interaction of gold and silver NPs with blood proteins was analyzed regarding their kinetic profile of the association/dissociation and dissociation constants (koff). The surface concentration density on the membrane composed of 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine and cholesterol (POPC/cholesterol) was 2.5 times higher than the value found after the injections of gold NPs on POPC only or with dimethyldioctadecylammonium (POPC/DDAB). Regarding the proteins, gold NPs showed preferential binding to fibrinogen resulting in a value of the variation of reflectivity that was 8 times higher than the value found for the other proteins. Differently, silver NPs showed similar interaction on all the tested proteins but with a variation of reflectivity on immunoglobulin G (IgG) 2 times higher than the value found for the other tested proteins