Spray-Freeze Drying: a Suitable Method for Aerosol Delivery of Antibodies in the Presence of Trehalose and Cyclodextrins
| Autor: | Alireza Vatanara, Behnaz Daneshmand, Maryam Amini Pouya, Homa Faghihi, Shabnam Aghababaie |
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| Rok vydání: | 2018 |
| Předmět: |
Materials science
Scanning electron microscope Size-exclusion chromatography Pharmaceutical Science 02 engineering and technology Aquatic Science 030226 pharmacology & pharmacy law.invention 03 medical and health sciences Freeze-drying chemistry.chemical_compound 0302 clinical medicine Differential scanning calorimetry Drug Stability law Drug Discovery medicine Crystallization Fourier transform infrared spectroscopy Ecology Evolution Behavior and Systematics Aerosols Cyclodextrins Ecology Trehalose General Medicine 021001 nanoscience & nanotechnology Freeze Drying Monomer chemistry Immunoglobulin G Mannitol Powders 0210 nano-technology Agronomy and Crop Science Nuclear chemistry medicine.drug |
| Zdroj: | AAPS PharmSciTech. 19:2247-2254 |
| ISSN: | 1530-9932 |
| DOI: | 10.1208/s12249-018-1023-2 |
| Popis: | We aimed to prepare spray-freeze-dried powder of IgG considering physicochemical stability and aerodynamic aspects. Spray-freeze drying (SFD) exposes proteins to various stresses which should be compensated by suitable stabilizers. The competence of cyclodextrins (CDs), namely beta-cyclodextrin (βCD) and hydroxypropyl βCD (HPβCD), at very low concentrations, was investigated in the presence of separate mannitol- and trehalose-based formulations. Spray-freeze-dried preparations were quantified in terms of monomer recovery and conformation by size exclusion chromatography (SEC-HPLC) and Fourier transform infrared (FTIR) spectroscopy, respectively. Differential scanning calorimetry (DSC) and X-ray diffractometry (XRD) were employed to identify the thermal characteristics of powders. Particle morphology was visualized by scanning electron microscopy (SEM). Aerodynamic behavior of powders was checked through an Anderson cascade impactor (ACI). Although all formulations protected antibody from aggregation during the SFD process (aggregation 1%), mannitol-containing ones failed upon the storage (19.54% in the worst case). Trehalose-HPβCD incomparably preserved the formulation with fine particle fraction (FPF) of 51.29%. Crystallization of mannitol resulted in IgG destabilization upon storage. Although employed concentration of CDs is too low (less than 50:1 molar ratio to protein), they successfully served as stabilizing agents in SFD with perfect improvement in aerosol functionality. Graphical Abstract ᅟ. |
| Databáze: | OpenAIRE |
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