Albumin binding onto synthetic vesicles

• DOI: 10.1039/c2sm26260f
• Publication Date: 2012-08-09T08:31:59Z
• Authors: Carlotta Pucci; Anita Scipioni; Camillo La Mesa
• Keywords: Surface charge; Random coil; Bovine serum albumin

Vesicular entities were obtained by mixing didodecyldimethylammonium bromide and sodium dodecylsulfate in non-stoichiometric ratios. The vesicles bear a positive surface charge, due to the cationic species being excess, adsorb significant amounts of protein, presumably electrostatic interactions. We modulated net charge bovine serum albumin pH observed its binding onto above vesicles. Binding is controlled albumin: it substantial when has negative charges excess negligible, or non-existent, below iso-electric point. For values >6.0, efficiency increases proportion protein charge. Surface coverage changes number neutralized upon remains same. size protein–vesicle lipo-plexes was inferred dynamic light scattering their ζ-potential. structure evaluated circular dichroism spectroscopy estimates α-helix, β-strand random coil contents achieved. Increasing subsequent suggests interaction between albumin. Attempts determine made elaborating ζ-potential values. results interpreted terms Gibbs adsorption isotherm. Accordingly, possible estimate energy under different conditions.