Abstract
This study focuses on hybrid vesicles (HVs) formed through co-assembly of soy phosphatidylcholine (SPC) and a triblock copolymer (F127). After elucidating the superior stability of HVs over the assemblies of neat SPC and F127, these were encapsulated with bovine serum albumin (BSA), as model a thermolabile protein. Characterizations were performed using dynamic light scattering (DLS), electron microscopy, circular dichroism and high-sensitivity differential scanning calorimetry. The size of HVs increased slightly at higher proportion of F127 and upon encapsulation of BSA. In spite of this, vesicles remained spherical and displayed a smooth surface. They showed superior dilution stability in comparison to neat copolymer micelles and phospholipid vesicles. Their stability can be ascribed to hydrophobic association between the phospholipid and copolymer, and manifested into increase in phase transition temperature of the former. We found that HVs could protect BSA from denaturation and unfolding when challenged by high solution temperature, pH changes and salt incorporation.
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