IMBICE   05372
INSTITUTO MULTIDISCIPLINARIO DE BIOLOGIA CELULAR
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Lyophilized nanoparticle albumin-based carrier: manufacturing and application for pulmonary route
Autor/es:
SIRI MACARENA; FERNANDEZ RUOCCO MARIA JULIETA; RISSO, VALERIA; CHIARAMONI, NADIA SILVIA; GRASSELLI, MARIANO; ALONSO, SILVIA DEL VALLE
Lugar:
Carlos Paz, Cordoba
Reunión:
Congreso; XLII Reunión Anula de la Sociedad Argentina de Biofísica; 2013
Institución organizadora:
Sociedad Argentina de Biofísica
Resumen:
The objective of this study was to investigate the stability of water soluble albumin nanoparticles as protein carrier and affinity drug for specific site with photosensitive marker MC 540. Lyophilized nanoparticles increased the mean sizes by approximately 30% after lyophilization, though this increase was statistically significant only for the nanoparticles at neutral pH. Merocynine (MC540) affinity for Sudlow I and II sites. Nanoparticles were prepared by Gamma irradiation of water-soluble serum albumin (BSA) with phosphate buffer and ethanol 40% (v/v). The BSAn nanoparticle was lyophilized after characterization as potential DDS as lyophilized powder. Also, conservation of structure-function characteristics were tested by activity site affinity of MC540, and as a selective marker. The size and Z potential of the nanoparticles were investigated after lyophilization by Light Scattering and Z Potential, 4th derivative UV-Vis spectroscopy, pH changes and Sudlow site affinity. Before lyophilization the particles were spherical in shape and had a smooth surface c.a. 20 nm and Z potential of -10 mV. The size range of the BSAn lyophilized was between 100 and 1000 nm and Z potential obtained was between 15 mV (pH=2) and -15 mV(pH=9). Result of the affinity studies showed that the BSAn lyophilized nanoparticles have an isosbestic point at 530 nm, point of enhance stability. The present study suggests that BSAn-lyo could be used for inhaled suspension for respiratory illness as a potential pulmonary protein delivery system (PPDS), according to findings that confirm that the stability of serum albumins is enhanced upon binding with the drug.