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Article dans une revue

Reversible protein precipitation to ensure stability during encapsulation within PLGA microspheres

Abstract :

Proteins were precipitated to ensure their stability upon subsequent encapsulation within PLGA microspheres. Spherical, nanosized protein particles were formed by the addition of a salt (sodium chloride) and a water-miscible organic solvent (glycofurol) to protein solutions. Various process parameters were modified to optimize the precipitation efficiency of four model proteins: lysozyme, alpha-chymotrypsin, peroxidase and beta-galactosidase. As monitored by enzymatic activity measurement of the rehydrated particles, conditions to obtain more than 95% of reversible precipitates were defined for each protein. The study of the structure of the rehydrated particles by absorbance spectroscopy, fluorescence spectroscopy and circular dichroism showed an absence of structural-perturbation after precipitation. Protein particles were then microencapsulated within PLGA microspheres using s/o/w technique. The average encapsulation yield was around 80% and no loss of protein activity occurred after the encapsulation step. Additionally, a lysozyme in vitro release study showed that all of the released lysozyme was biologically active. This method of protein precipitation is appropriate for the encapsulation in PLGA microspheres of various proteins without inactivation.

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Article dans une revue
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https://hal.univ-angers.fr/hal-03171796
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Soumis le : mercredi 17 mars 2021 - 11:12:43
Dernière modification le : jeudi 8 juillet 2021 - 13:38:01

Identifiants

  • HAL Id : hal-03171796, version 1
  • OKINA : ua3772

Citation

A. Giteau, Marie-Claire Venier-Julienne, Stephane Marchal, Jean-Luc Courthaudon, M. Sergent, et al.. Reversible protein precipitation to ensure stability during encapsulation within PLGA microspheres. European Journal of Pharmaceutics and Biopharmaceutics, Elsevier, 2008, 70, pp.127-136. ⟨hal-03171796⟩

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