The effect of lauryl capping group on protein release and degradation of poly(d,l-lactic-co-glycolic acid) particles

The effect of lauryl capping group on protein release and degradation of poly(d,l-lactic-co-glycolic acid) particles

The aim of this study was to investigate the effect of a specific and frequently used end group (lauryl alcohol) on the protein release and degradation kinetics of poly(DL-lactic-co-glycolic acid) particles of different sizes. Lauryl-capped PLGA and uncapped PLGA (referred to as PLGA-capped and PLGA...

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Bibliographic Details
Published in:Journal of controlled release Vol. 172; no. 2; pp. 436 - 443
Main Authors: Samadi, N., Abbadessa, A., Di Stefano, A., van Nostrum, C.F., Vermonden, T., Rahimian, S., Teunissen, E.A., van Steenbergen, M.J., Amidi, M., Hennink, W.E.
Format: Journal Article
Language:English
Published: Netherlands Elsevier B.V 10-12-2013
Subjects:
alcohols
Animals
Bovine serum albumin
Cattle
Degradation
Dodecanol - chemistry
Dodecanol - metabolism
Drug Carriers - chemistry
Drug Carriers - metabolism
emulsions
evaporation
Fourier transform infrared spectroscopy
glycolic acid
Hydrolysis
hydrophobicity
lactic acid
Lactic Acid - chemistry
Lactic Acid - metabolism
Microparticles
Nanoparticles
Particle Size
PLGA
Polyglycolic Acid - chemistry
Polyglycolic Acid - metabolism
polymers
Release
Serum Albumin, Bovine - administration & dosage
solvents
Degradation
Nanoparticles
Bovine serum albumin
PLGA
Release
Microparticles
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Summary:The aim of this study was to investigate the effect of a specific and frequently used end group (lauryl alcohol) on the protein release and degradation kinetics of poly(DL-lactic-co-glycolic acid) particles of different sizes. Lauryl-capped PLGA and uncapped PLGA (referred to as PLGA-capped and PLGA-COOH, respectively) particles (0.3, 1 and 20μm) were prepared by a double emulsion solvent evaporation technique. Bovine serum albumin (BSA) was used as a model protein for release studies. During degradation (PBS buffer, pH7.4 at 37°C), a slower dry mass loss was observed for 0.3μm particles than for particles of 1 and 20μm. It was further shown that PLGA-capped particles showed slower mass loss likely due to its more hydrophobic nature. It was found that the ester bond hydrolysis rate was substantially slower for PLGA-capped particles and that the rate increased with particle size. Particles showed enrichment in lactic acid content (and thus a decrease in glycolic acid content) in time, and interestingly PLGA-capped particles showed also an enrichment of the lauryl alcohol content. No difference was observed in degradation kinetics between BSA loaded and blank particles. Independent of size, PLGA-COOH based particles showed, after a small burst, a sustained and nearly complete release of BSA during 60–80days. On the other hand, particles based on PLGA-capped showed a much slower release and exhibited incomplete release, accompanied by the presence of an insoluble residue remaining even after 180days. FTIR analysis of this residue showed that it contained both polymer and protein. Considering the polymer enrichment in lauryl alcohol, the incomplete release observed for PLGA-capped is likely attributed to interactions between the protein and the lauryl end group. In conclusion, since PLGA-COOH, in contrast to the capped derivative, shows complete degradation as well as quantitative release of an entrapped protein, this polymer is preferred for the design of protein formulations. [Display omitted]
Bibliography:http://dx.doi.org/10.1016/j.jconrel.2013.05.034
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ISSN:0168-3659
1873-4995
DOI:10.1016/j.jconrel.2013.05.034