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Aqueous two-phase systems as a formulation concept for spray-dried protein

Elversson, Jessica and Millqvist-Fureby, Anna LU (2005) In International Journal of Pharmaceutics 294(1-2). p.73-87
Abstract

This study investigates to what extent an aqueous two-phase system (ATPS) can encapsulate and protect the secondary structure of a protein during spray drying. The ATPSs contained polyvinyl alcohol (PVA) and dextran solutions, in different proportions. A model protein, bovine serum albumin (BSA) and, in some experiments, trehalose were added to the ATPS prior to spray drying. Electron spectroscopy for chemical analysis (ESCA), differential scanning calorimetry (DSC), UV spectrophotometry, size exclusion high-performance liquid chromatography (SEC-HPLC) and Fourier transform infrared spectroscopy (FTIR) were used for analysis of solid and reconstituted samples. The anticipated function of the ATPS was to improve the stability of the... (More)

This study investigates to what extent an aqueous two-phase system (ATPS) can encapsulate and protect the secondary structure of a protein during spray drying. The ATPSs contained polyvinyl alcohol (PVA) and dextran solutions, in different proportions. A model protein, bovine serum albumin (BSA) and, in some experiments, trehalose were added to the ATPS prior to spray drying. Electron spectroscopy for chemical analysis (ESCA), differential scanning calorimetry (DSC), UV spectrophotometry, size exclusion high-performance liquid chromatography (SEC-HPLC) and Fourier transform infrared spectroscopy (FTIR) were used for analysis of solid and reconstituted samples. The anticipated function of the ATPS was to improve the stability of the protein by preventing interactions with the air-liquid interface during drying and by improving the encapsulation of the protein in the dried powder. BSA was found to preferentially partition to the dextran phase and in the absence of PVA, BSA dominated the powder surface. In samples containing PVA, the polymer mainly covered the powder surface, even though the dextran-rich phase was continuous, thus preventing protein surface interactions and providing improved encapsulation. However, PVA was found to cause partial loss of the native structure of BSA although the protein was well encapsulated during spray drying.

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author
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publishing date
type
Contribution to journal
publication status
published
keywords
Aqueous two-phase system, Bovine serum albumin, Electron spectroscopy for surface analysis, Encapsulation, Fourier transform infrared spectroscopy, Protein formulation, Spray drying, Trehalose
in
International Journal of Pharmaceutics
volume
294
issue
1-2
pages
15 pages
publisher
Elsevier
external identifiers
  • scopus:16344369715
  • pmid:15814232
ISSN
0378-5173
DOI
10.1016/j.ijpharm.2005.01.015
language
English
LU publication?
no
id
0b3e15a5-9b33-4ada-8d7b-cef40854fd37
date added to LUP
2025-04-14 17:19:47
date last changed
2025-04-23 11:02:16
@article{0b3e15a5-9b33-4ada-8d7b-cef40854fd37,
  abstract     = {{<p>This study investigates to what extent an aqueous two-phase system (ATPS) can encapsulate and protect the secondary structure of a protein during spray drying. The ATPSs contained polyvinyl alcohol (PVA) and dextran solutions, in different proportions. A model protein, bovine serum albumin (BSA) and, in some experiments, trehalose were added to the ATPS prior to spray drying. Electron spectroscopy for chemical analysis (ESCA), differential scanning calorimetry (DSC), UV spectrophotometry, size exclusion high-performance liquid chromatography (SEC-HPLC) and Fourier transform infrared spectroscopy (FTIR) were used for analysis of solid and reconstituted samples. The anticipated function of the ATPS was to improve the stability of the protein by preventing interactions with the air-liquid interface during drying and by improving the encapsulation of the protein in the dried powder. BSA was found to preferentially partition to the dextran phase and in the absence of PVA, BSA dominated the powder surface. In samples containing PVA, the polymer mainly covered the powder surface, even though the dextran-rich phase was continuous, thus preventing protein surface interactions and providing improved encapsulation. However, PVA was found to cause partial loss of the native structure of BSA although the protein was well encapsulated during spray drying.</p>}},
  author       = {{Elversson, Jessica and Millqvist-Fureby, Anna}},
  issn         = {{0378-5173}},
  keywords     = {{Aqueous two-phase system; Bovine serum albumin; Electron spectroscopy for surface analysis; Encapsulation; Fourier transform infrared spectroscopy; Protein formulation; Spray drying; Trehalose}},
  language     = {{eng}},
  month        = {{04}},
  number       = {{1-2}},
  pages        = {{73--87}},
  publisher    = {{Elsevier}},
  series       = {{International Journal of Pharmaceutics}},
  title        = {{Aqueous two-phase systems as a formulation concept for spray-dried protein}},
  url          = {{http://dx.doi.org/10.1016/j.ijpharm.2005.01.015}},
  doi          = {{10.1016/j.ijpharm.2005.01.015}},
  volume       = {{294}},
  year         = {{2005}},
}