AI Article Synopsis

  • A novel pharmaceutical vehicle was created using liposomes encapsulated with unmodified albumin and characterized through various techniques like microscopy and dynamic light scattering.
  • The study focused on vancomycin as a model drug, revealing that liposomes could be effectively trapped in albumin microspheres, with factors like zeta potential and albumin concentration affecting drug entrapment efficiency (which ranged from 13.17% to 61.27%).
  • The findings highlighted the interplay between liposome composition, microsphere zeta potential, and protein concentration, showcasing the potential for these vehicles in versatile drug delivery applications.

Article Abstract

A pharmaceutical vehicle based on the encapsulation of liposomes with unmodified albumin has been designed, formulated, and in vitro characterized. Microscopy was used to investigate particle morphology and dynamic light scattering to determine the size and zeta potential. Vancomycin was selected as a model drug for water-soluble and moderately albumin-bound products. The results indicated that regardless of the zeta potential of the liposomes these can be trapped within albumin microspheres. The zeta potential, drug entrapment efficacy, and drug delivery profile of the resulting microspheres were found to depend on the liposome composition and the conditions of flocculation. The protein concentration was observed to influence drug entrapment efficiency (from 13.17 ± 5.0% to 61.27 ± 4.54%), as did the zeta potential of the microspheres, which was also seen to depend on the initial charge of the liposomes. The relationship between the microsphere zeta potential or entrapment efficacy and the protein concentration used for flocculation was established. Regarding drug delivery, differences between microspheres prepared from cationic or anionic liposomes were observed. The combination of liposome versatility together with the drug-binding ability of albumin provides to a vehicle with multiple choices for theranostic delivery.

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http://dx.doi.org/10.1016/j.xphs.2016.05.009DOI Listing

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