INFLUENCE OF SHAKING AND SURFACTANTS ON THE RELEASE OF BSA FROM PLGA MICROSPHERES

Citation
Rm. Hernadez et al., INFLUENCE OF SHAKING AND SURFACTANTS ON THE RELEASE OF BSA FROM PLGA MICROSPHERES, European journal of drug metabolism and pharmacokinetics, 23(2), 1998, pp. 92-96
Citations number
16
Categorie Soggetti
Pharmacology & Pharmacy
ISSN journal
03787966
Volume
23
Issue
2
Year of publication
1998
Pages
92 - 96
Database
ISI
SICI code
0378-7966(1998)23:2<92:IOSASO>2.0.ZU;2-2
Abstract
The aim of the present work was to study the release of a model protei n, bovine serum albumin (BSA) encapsulated within biodegradable poly ( D,L-lactide-co-glycolide) (PLGA) microspheres prepared by a modified s olvent evaporation method using a double emulsion. These microspheres were characterized for size, morphology, surface adsorbed protein, enc apsulation efficiency and release kinetics. Two types of in vitro assa ys were developed to evaluate the influence of shaking and the additio n of surfactants on the release profile of encapsulated protein. Scann ing electron microscopy (SEM) observation showed spherical and smooth surface particles, with a mean particle size of 20 mu m and an encapsu lation efficiency of 81%. Surface associated protein was about 25%. Th e in vitro release profile showed a biphasic pattern described by mean s of a biexponential equation. There was an initial burst effect due t o the release of the protein adsorbed on the microsphere surface and a sustained release phase due to protein diffusion through the channels or pores formed in the polymer coat. The release obtained profiles in static and dynamic assays showed statistically significant difference s in the amount of the released protein, whereas the release rate was not affected. The burst effect was 28.30+/-1.63% and 35.20+/-1.50% of the total encapsulated protein for the static and dynamic assays respe ctively. The addition of surfactants (SDS) to the release medium incre ased the rate and the amount of drug released. In both assays the valu e of the slow release rate constant, beta, was 0.029+/-0.002 days(-1) when the surfactant was added, and 0.017+/-0.0014 days(-1) in the samp les without surfactant. It is believed that the surfactant leads to an increase in the microsphere surface polarity which allows channel and pore formation inside the polymer through which the protein diffuses easily.