Bovine Serum Albumin Nanoparticle (BNp): Structure/Function

MACARENA SIRI; GABRIELA TORCHIO; RAMIRO LLOVERA; JUAN FRANCISCO DELGADO; MARIANO GRASELLI; SILVIA DEL VALLE ALONSO

Sierra de la Ventana

Simposio; XLIII Reunión anual de la Sociedad Argentina de Biofísica; 2014

Sociedad Argentina de Biofísica

A new nanoparticle made from bovine serum albumin (BSA) was characterized as a possible carrier for a drug delivery system. The nanoparticle was obtained according to Soto Espinoza et al., 2012. BNp spectroscopic studies were carried out by UV-Visible, Fluorescence, FTIR, DLS and Z potential, microscopy (TEM) and surface characterization (amino groups, thiols and carbonyls detection). The stability of the BNp was also studied by pH, different detergents and temperature. Freeze-drying was studied as a possible way of BNp storage. The product was studied by SEM, UV-Visible, 4th derivative and fluorescence. The lyophilisation process gave particles of larger size (40 nm, 130 nm y 350 nm). Lastly, a drug of choice (Emodin) was carrier-encapsulated in order to test its structure/function as a drug delivery system. Assays on encapsulation under different conditions, release kinetic profile and saturation curve by fluorescence were carried out. Results showed the existence of the nanoparticle (with a slightly elliptic shape), which has a size between 20 ? 70 nm. By spectroscopy assays BSA molecules forming the BNp, conserved a similar protein structure and stability. Differences appeared in the surface characterization where the free thiols on the BNp differed in quantity from those in the molecule, c.a. doubling it. As regards the encapsulation process, room temperature and 15 minutes of incubation was the most efficient condition (79%). The release kinetic profile was similar to that of the BSA. The saturation curve showed similar results between both systems tested.