Estudo da interação entre albumina do soro bovino (BSA) e nanopartículas de maghemita (Y-Fe2O3) funcionalizadas com três diferentes ligantes aniônicos

• Autor(a) principal: Silva, Sueli Maria da
• Data de Publicação: 2017
• Tipo de documento: Tese
• Idioma: por
• Título da fonte: Repositório Institucional da UFG
• dARK ID: ark:/38995/0013000008xhk
• Texto Completo: http://repositorio.bc.ufg.br/tede/handle/tede/7803
• topic: Nanopartícula; Maghemita; Proteína; Ligante; Protein; Nanoparticle; Maghemite; Ligand; CIENCIAS EXATAS E DA TERRA::QUIMICA

Biological applications of nanoparticles require understanding the interaction between proteins and nanoparticles. In this thesis were performed studies of interaction between the protein BSA and maghemite nanoparticles functionalized with different anionic ligands (citrate ions, tripolyphosphate ions and bilayer laurate ions ), by three analytical techniques: isothermal titration calorimetry (ITC), adsorption isotherm by hydrodynamic diameter measurements using dynamic light scattering (DLS) and fluorescence spectroscopy. The values of the interaction constants (Ka) of BSA association on nanoparticles surface by DLS measurements were similar to those obtained by ITC, for the three systems. On the other hand, the study by ITC did not allows determining of the stoichiometry values (Nmax) of the association processes. The results obtained by the fluorescence technique are highly discrepant of the results obtained by the other two techniques. The evaluation of the functionalizing agent effect on the interaction between magnetite nanoparticles and BSA showed that there are differences in the Ka values, and in the energetic profiles of the interactions for the three systems studied. The Ka value for the interaction between BSA and citrate functionalized nanoparticles was in the order of 106 M-1, whereas for the other systems the values of Ka were 104 M-1. The energetic profile of the interactions, was endothermic in the system BSA-NP-Citrate, and exothermic for BSA-NP-Laurato and for BSA-NP-Tripolyphosphate. From the analysis of the thermodynamic parameters, it was possible to suggest that the interaction in the BSA-NP-citrate system was predominantly electrostatic, whereas the interaction in the other systems predominantly involved hydrogen bonds. The albumin estearase activity was reduced by the interaction with the nanoparticles, and was dependent upon the nanoparticles concentration. The reduction in stearase activity was higher for the -BSA-NP-Laurate system. In this work, the dynamic light scattering technique (DLS) was used, for the first time, to study of adsorption of BSA on functionalized maghemite nanoparticles. In addition, under the experimental conditions used, DLS was the only technique that provided (Nmax) values similar to those estimated.