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
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.