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  • 1
    Electronic Resource
    Electronic Resource
    Release of Human Serum Albumin from Poly(lactide-co-glycolide) Microspheres (1990)
    Springer
    Pharmaceutical research 7 (1990), S. 1190-1194 
    Details
    ISSN: 1573-904X
    Keywords: protein release ; human serum albumin ; protein stability ; biodegradable microspheres ; poly(lactide-co-glycolide)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Human serum albumin (HSA) was encapsulated in a 50:50 copolymer of DL-lactide/glycolide in the form of microspheres. These microspheres were used as a model formulation to study the feasibility of controlling the release of large proteins over a 20- to 30-day period. We show that HSA can be successfully incorporated into microspheres and released intact from these microspheres into various buffer systems at 37°C. A continuous release of the protein could be achieved in physiological buffers at 37°C over a 20- to 30-day period from microspheres with high protein loadings (11.6%). These results demonstrate the potential of poly(DL-lactide-co-glycolide) microspheres for continuous delivery of large proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015948829632
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  • 2
    Electronic Resource
    Electronic Resource
    Lyophilized Formulations of Recombinant Tumor Necrosis Factor (1992)
    Springer
    Pharmaceutical research 9 (1992), S. 33-36 
    Details
    ISSN: 1573-904X
    Keywords: tumor necrosis factor ; protein formulations ; lyophilization of proteins ; amorphous protectants ; nonreducible oligomers
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Recombinant tumor necrosis factor-alpha (TNF), an investigational biological response modifier, is a protein and is susceptible to particulate generation during handling in dilute aqueous solutions. TNF is prone to formation of nonreducible dimers and oligomers during formulation, lyophilization, and storage. The effect of various parameters, such as the pH, protein concentration, and nature of excipients present during lyophilization, on the formation of nonreducible dimers and oligomers was investigated. The results of these studies indicate that these parameters can significantly alter the rate of this reaction. Inclusion of an amorphous buffer and an appropriate amount of a crystallizing sugar (mannitol) combined with a suitable quantity of an amorphous protectant (dextran, sucrose, trehalose, or 2-hydroxypropyl-β-cyclodextrin) was shown to reduce the formation of these dimeric and oligomeric species during lyophilization. Representative lyophilized formulations of TNF based on selected amorphous excipients were found to be fully bioactive and stable over 9 months.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018919508463
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  • 3
    Electronic Resource
    Electronic Resource
    Use of 2-Hydroxypropyl-β-cyclodextrin as a Solubilizing and Stabilizing Excipient for Protein Drugs (1991)
    Springer
    Pharmaceutical research 8 (1991), S. 792-795 
    Details
    ISSN: 1573-904X
    Keywords: 2-hydroxypropyl-β-cyclodextrin ; ovine growth hormone ; interleukin-2 ; insulin ; stability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A chemically modified, amorphous β-cyclodextrin, namely, 2-hydroxypropyl-β-cyclodextrin (HPCD), was examined as a solubilizing and stabilizing agent for protein drugs. The aqueous solubility of ovine growth hormone at pH 7.4 was increased through the use of HPCD. This effect was manifested by higher UV transparency at 600 nm. Interleukin-2 (IL-2) is rendered insoluble upon lyophilization in the absence of stabilizers. Use of aqueous HPCD provides a clear solution, as indicated by fluorometric light scattering, and inhibits aggregate formation, as shown by ultracentrifugation and Western blot analyses. In addition, there were no major conformational changes of IL-2 in HPCD formulation as indicated by fourth-derivative ultraviolet spectroscopy. Finally, IL-2 retained 100% of its biopotency when prepared in HPCD solutions. Aggregation of insulin was also suppressed by HPCD. These data, as well as the i.v. safety of HPCD and its well-characterized chemical composition, suggest that this starch derivative may be a potentially useful excipient for protein drugs intended for parenteral use.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015870521744
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