Development of double emulsion nanoparticles for the encapsulation of bovine serum albumin

• Published in: Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2017-10, Vol.158, p.190-196
• Main Authors: Martinez, Nelida.Y., Andrade, Patricia F., Durán, Nelson, Cavalitto, Sebastian
• Format: Article
• Language: English
• Subjects: Animals; Bovine serum albumin encapsulation; Cattle; Double emulsion nanoparticles; Emulsions - chemistry; Hydrophobic and Hydrophilic Interactions; Hydrophobic interactions; Nanoparticles - chemistry; Pluronic F68; Poloxamer - chemistry; Poly-ε-caprolactone; Serum Albumin, Bovine - chemistry; Spectroscopy, Fourier Transform Infrared
• ISSN: 0927-7765; 1873-4367
• DOI: 10.1016/j.colsurfb.2017.06.033

[Display omitted] •Double emulsion nanoparticles size ranges from 300 to 500nm.•The polydispersity index varies with the concentration of surfactant.•Hydrophobic interactions are present between BSA and the matrix.•Sonication slightly affects the secondary structure of BSA.•FTIR studies confirmed the presence of BSA in the nanoparticles. In the present work, a double emulsion was developed for the encapsulation of Bovine Serum Albumin (BSA) as a model protein for the future encapsulation of viral proteins. The first emulsion polydispersity index (PDI) was studied with increasing concentrations of poly (ε-caprolactone) (PCL) as stabilizer (from 16% w/v to 5% w/v) and polyvinyl alcohol (PVA) as the surfactant in the second emulsion at 1.5% w/v. Results suggest that at decreasing concentrations of PCL the PDI of the emulsion also decrease, indicating that viscosity of the emulsion is crucial in the homogeneity of the resultant size distribution of the nanoparticles. When PVA concentration in the second emulsion was increased from 1.5% w/v to 2.5% w/v the PDI also increased. To study the relationship between the structure of the surfactant in the second emulsion and the resultant BSA encapsulation, emulsions were prepared with Pluronic F68 and PVA both at 1.5% w/v and PCL in the first emulsion at 5% w/v. Results indicated that Pluronic F68 was a better stabilizer because at the same experimental conditions encapsulation of BSA was 1.5 higher than PVA. FTIR studies confirmed the presence of BSA in the nanoparticles. SEM and TEM microscopies showed a size distribution of 300nm–500nm size of nanoparticles. Circular dichroism studies demonstrated that the secondary structure of the protein was conserved after the encapsulation into the nanoparticles.