Effect of particle functionalization and solution properties on the adsorption of bovine serum albumin and lysozyme onto silica nanoparticles

Autor(es)

Galdino, Flavia Elisa ^{[1, 2]} ; Picco, Agustin Silvio ^{[2, 3]} ; Sforca, Mauricio Luis ^[4] ; Cardoso, Mateus Borba ^{[1, 2]} ; Loh, Watson ^[1]

Afiliação do(s) autor(es)

^[1] Univ Estadual Campinas, Inst Chem, UNICAMP, CP 6154, BR-13083970 Campinas, SP - Brazil

^[2] Natl Ctr Res Energy & Mat CNPEM, Brazilian Nanotechnol Natl Lab LNNano, CP 6154, BR-13083970 Campinas, SP - Brazil

^[3] Univ Nacl La Plata, CONICET, Fac Cs Exactas, Inst Invest Fisicoquim Teor & Aplicadas INIFTA, 64 & Diag 113, RA-1900 La Plata - Argentina

^[4] Natl Ctr Res Energy & Mat CNPEM, Brazilian Biosci Lab LNBio, CP 6154, BR-13083970 Campinas, SP - Brazil

• Tipo de documento: Artigo Científico
• Fonte: COLLOIDS AND SURFACES B-BIOINTERFACES; v. 186, FEB 2020.
• Citações Web of Science: 0

Resumo

Silica nanopartides present an enormous potential as controlled drug delivery systems with high selectivity towards diseased cells. This application is directly related to the phenomenon of protein corona, characterized by the spontaneous adsorption of proteins on the nanoparticle surface, which is not fully understood. Here, we report an investigation on the influence of pH, ionic strength and temperature on the thermodynamics of interaction of bovine serum albumin protein (BSA) with non-functionalized silica nanoparticles (SiO(2)NPs). Complementary, we also investigated the ability of polyethylene glycol (PEG) and zwitterionic sulfobetaine (SBS) surface-modified nanoparticles to prevent the adsorption of BSA (protein negatively charged at physiological pH) and lysozyme (protein positively charged at physiological pH). We showed that BSA interaction with SiO2 NPs is enthalpically governed. On the other hand, functionalization of silica nanoparticles with PEG and SBS completely prevented BSA adsorption. However, these functionalized nanopartides presented a negative zeta potential and were not able to suppress lysozyme anchoring due to strong nanoparticle-protein electrostatic attraction. Due to the similarity of BSA with Human Serum Albumin, this investigation bears a resemblance to processes involved in the phenomenon of protein corona in human blood, producing information that is relevant for the future biomedical use of functionalized nanoparticles. (AU)

• Processo FAPESP: 14/21910-8 - Evolução das nanopartículas de sílica em meios biológicos: estudo sobre a formação da coroa de proteína, da agregação e captação celular
• Beneficiário: Agustín Silvio Picco
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado
• Processo FAPESP: 16/11118-0 - Estudo da interação de proteínas com nanopartículas de sílica: termodinâmica da interação e efeito da superfície das partículas
• Beneficiário: Flávia Elisa Galdino
• Modalidade de apoio: Bolsas no Brasil - Mestrado
• Processo FAPESP: 15/25406-5 - Organizando a matéria: colóides formados por associação de surfactantes, polímeros e nanopartículas
• Beneficiário: Watson Loh
• Modalidade de apoio: Auxílio à Pesquisa - Temático