Adsorption of BSA (Bovine Serum Albuminum) and lysozyme on poly(vinyl acetate) particles

Abstract

SbstractPoly(vinyl acetate) (PVAc) particles find many uses in the biomedical field, including the use as particle embolizers. Particularly, embolizing particles can combine physical and chemical effects when they are doped with pharmaceuticals. For this reason, the adsorption of bovine serum albuminum (BSA) and lysozyme (used as model biomolecules) on PVAc particles produced through suspension polymerization is studied in the present manuscript in a broad range of pH values. It is shown that significant amounts of BSA and lysozyme can be adsorbed onto PVAc particles in the vicinities of the isoelectric point of the biomolecules (0.65mg of BSA and 1.0mg of lysozyme per g of PVAc), allowing for production of chemoembolizers through adsorption. Particularly, it is shown that lysozyme still presents residual activity after the adsorption process, which can constitute very important characteristic for real biomedical applications.

Probing the behavior and kinetic studies of amphiphilic acrylate copolymers with bovine serum albumin

“…BSA has been the most studied protein in adsorption–desorption process as a function of charge, protein concentration, pH, substrate charge and polarization potential, permitting studies in the presence and absence of charge 21 , 22 . Bovine serum albumin (BSA) has poorer internal stability than other proteins, it was selected as the model protein for the adsorption studies 23 . Higher internal stability proteins exclusively adsorb onto hydrophilic surfaces via electrostatic interactions, whereas lower internal stability proteins adsorb onto any surface independent of electrostatic connections 24 .…”

Probing the binding behavior and kinetic studies of amphiphilic acrylate copolymers with bovine serum albumin

“…Higher internal stability proteins exclusively adsorb onto hydrophilic surfaces via electrostatic interactions, whereas lower internal stability proteins adsorb onto any surface independent of electrostatic connections [12]. Because bovine serum albumin (BSA) has poorer internal stability than other proteins, it was selected as the model protein for the adsorption studies [13]. BSA protein is highly demanded by researchers and frequently used because of its high purity and water solubility [14].…”