The critical need for robust assays for quantitation and characterization of aggregates of therapeutic proteins. Analysis of aggregates and particles in protein pharmaceuticals. New Jersey: John Wiley and Sons; Nafissi-Varcheh N, Aboofazeli R. An approach to the design of a particulate system for oral protein delivery. Preparation and stability study of rhGH-loaded in simulated gastrointestinal fluids.
Temperature- and pH-induced multiple partially unfolded states of recombinant human interferon-alpha2a: Possible implications in protein stability. Evaluating the effects of buffer conditions and extremolytes on thermostability of granulocyte colony-stimulating factor using high-throughput screening combined with design of experiments.
Relevant shaking stress conditions for antibody preformulation development. Preparing poly lactide-co-glycolic acid PLGA microspheres containing lysozyme-zinc precipitate using a modified double emulsion method. Purification and conformational properties of a human interferon alpha2b produced in Escherichia coli.
Characterizing Nanoparticles in Liquids: Protein Aggregation Studies
Isolation and characterization of a monomethioninesulfoxide variant of interferon alpha- 2b. Molecular and biologic characterization of recombinant interferon-alpha2b. Yuen P, Kline D, inventors. Stable aqueous alpha interferon solution formulations. US Patent. Isaacs A, Lindenmann J.
Virus interference. The interferon.
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- Analysis of Aggregates and Particles in Protein Pharmaceuticals.
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At least three human type alpha interferons: Structure of alpha 2. Long-term stabilization of recombinant human interferon alpha 2b in aqueous solution without serum albumin. Protein aggregates seem to play a key role among the parameters influencing the antigenicity of interferon alpha IFN-alpha in normal and transgenic mice.
Structural characterization and immunogenicity in wild-type and immune tolerant mice of degraded recombinant human interferon alpha2b. Ultraviolet absorption spectroscopy.
Protein Aggregation Characterization
Methods for structural analysis of protein pharmaceuticals. Biotechnology: Pharmaceutical aspects. Press; Esfandiary R, Middaugh CR. In: Mahler HC, jiskoot W, editors. Analysis of aggregation and particles in protein pharamaceuticals. Development of a high performance size exclusion chromatography method to determine the stability of human serum albumin in a lyophilized formulation of interferon alfa-2b.
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- Determining onset of protein aggregation.
Chromatographic methods for quantitative analysis of native, denatured, and aggregated basic fibroblast growth factor in solution formulations. Rationalization of the effects of mutations on peptide and protein aggregation rates. Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering. Suppression of insulin aggregation by heparin.
Electrostatically driven protein aggregation: beta-lactoglobulin at low ionic strength. Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor. Chemical and physical stability of chimeric L6, a mouse-human monoclonal antibody. The effects of formulation variables on the stability of freeze-dried human growth hormone. Quantifying sub-micrometer particles in protein therapeutics is a potential of the FFF technique that is yet to be realized, due to the lack of detection with sufficient sensitivity.
In this article the effect of several important parameters on the optimization of FFF analyses are explored, and the strengths, weaknesses, and potential new applications of the technique are discussed. Affiliation: Amgen Inc.
Abstract: Field flow fractionation FFF is a technique that holds great promise for the analysis and characterization of protein aggregates and particles, due to its wide dynamic range and matrix-free separation mechanism. Journal Name: Current Pharmaceutical Biotechnology. Volume 10 , Issue 4 , Next, it covers:. Methods to detect and measure soluble aggregates based on separation, light scattering, and new technology.
Approaches for managing aggregates and particles found during protein purification and formulation development. Throughout the text, case studies help researchers deal with the challenges that arise in detecting and analyzing protein aggregates and particles. Protein pharmaceuticals are increasingly used to treat life-threatening and chronic diseases, including cancer, viral infections, metabolic disorders, and central nervous system diseases. With Analysis of Aggregates and Particles in Protein Pharmaceuticals as their guide, pharmaceutical researchers now have an important tool in overcoming the challenging problem of aggregates and particles in protein drug development.
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