TY - JOUR ID - 10442/16881 A1 - Papagiannopoulos A. Y1 - 2018/// T1 - Bovine serum albumin interactions with cationic surfactant vesicles decorated by a low-molar-mass polysaccharide JF - Colloids and Surfaces A: Physicochemical and Engineering Aspects VL - 537 SN - 0927-7757 U3 - 10.1016/j.colsurfa.2017.10.058 PB - Elsevier B.V. SP - 495–501EP - UR - https://hdl.handle.net/10442/16881 N2 - The complexation of bovine serum albumin (BSA) with bare and sodium-hyaluronate (Na-HA)-modified didodecyldimethylammonium bromide (DDAB) vesicles is systematically investigated by static and dynamic light scattering in a broad range of scattering angles. The aggregation number of DDAB vesicles increases as a function of added Na-HA concentration because of the attractive interactions between the cationic surfactant and anionic polysaccharide that reduce the repulsions between the charged head groups of the surfactant. This is confirmed by the inversion of the vesicular surface charge upon addition of Na-HA. Interactions of BSA with DDAB vesicles are surprisingly found to be much stronger when Na-HA is adsorbed on the vesicles although in this case protein and vesicular surface charge are of the same sign. Apparently the anisotropically charged BSA globules are more effectively anchored on the complex interface of the Na-HA decorated DDAB vesicles in comparison to the uniform positively charged interface of bare DDAB vesicles. In addition the strong associations of the globular protein with the vesicles compromise the protein’s secondary structure. This system can be a useful template for versatile nanocapsules with the ability to bind substances via hydrophobic and electrostatic interactions. ER -