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Thursday, July 23, 2020 | History

3 edition of Investigation of the Freeze-Thawing Process for Pharmaceutical Formulations of a Model Protein found in the catalog.

Investigation of the Freeze-Thawing Process for Pharmaceutical Formulations of a Model Protein

Anna Hillgren

Investigation of the Freeze-Thawing Process for Pharmaceutical Formulations of a Model Protein

by Anna Hillgren

  • 94 Want to read
  • 39 Currently reading

Published by Uppsala Universitet .
Written in English

    Subjects:
  • Pharmacology,
  • Medical

  • Edition Notes

    SeriesComprehensive Summaries of Uppsala Dissertations from the Faculty of Pharmacy, 272
    The Physical Object
    FormatPaperback
    Number of Pages48
    ID Numbers
    Open LibraryOL12854511M
    ISBN 10915545304X
    ISBN 109789155453046

      Here we presented an efficient method for mild solubilization of inclusion bodies by using a freeze-thawing process in the presence of low concentration of urea. We used two different proteins to demonstrate the advantage of this method over the traditional urea-denatured method: enhanced green fluorescent protein (EGFP) and the catalytic. Saccharides, including sucrose, trehalose, mannitol, and sorbitol, are commonly employed as stabilizers, cryoprotectants, and/or tonicity adjusters in protein formulations. During the thawing of a protein-containing formulated bulk drug substance.

    Deep eutectic solvents for pharmaceutical formulation and drug delivery applications. Shahram Emami & Ali Shayanfar. Pages: A model-based approach for the rational design of the freeze-thawing of a protein-based formulation. Andrea Arsiccio, Livio Marenco & .   Summary This chapter contains sections titled: Introduction The Basics of Freezing Nonequilibrium Freezing and State Diagrams Freezing Freezing of Biologicals Freeze–Thaw Processing of Protein Solu.

    Use risk assessment to prioritize knowledge gaps for further investigation; Design a formulation and identify the critical material (quality) attributes of the final product that must be controlled to meet the target product quality profile. Design a manufacturing process to produce a final product having these critical material attributes. A mathematical model that simulates temperature profiles during freezing process of standard pharmaceutical formulations was set up, and the ice crystal mean sizes were semi empirically estimated from the resulting temperature profiles. It was confirmed that, for a given formulation, the mass transfer parameters during freeze-drying were.


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Investigation of the Freeze-Thawing Process for Pharmaceutical Formulations of a Model Protein by Anna Hillgren Download PDF EPUB FB2

Recent advances in recombinant DNA technology have resulted in a great number of proteins with a potential to enter pharmaceutical formulations.

The most commonly used method for preparing protein pharmaceuticals is by freeze-drying. Freezing is an important step in this process and therefore a deeper investigation of the freeze-thawing process is by: 2.

The most commonly used method for preparing protein pharmaceuticals is by freeze-drying. Freezing is an important step in this process and therefore a deeper investigation of the freeze-thawing process is qualified. The aim of the thesis was to investigate the protection of protein during freeze-thawing.

Investigation of the Freeze-Thawing Process for Pharmaceutical Formulations of a Model Protein. By Anna Hillgren. Abstract. Freezing is an important step in this process and therefore a deeper investigation of the freeze-thawing process is qualified. The aim of the thesis was to investigate the protection of protein during : Anna Hillgren.

Hillgren, A., Investigation of the Freeze-Thawing Process for Pharmaceutical Formulations of a Model Protein. Acta Universitatis Upsaliensis. Comprehensive Summaries of Uppsala Dissertations from the Faculty of Pharmacy 48 pp. Uppsala. ISBN X. Recent advances in recombinant DNA technology have resulted in a great number of.

Lactate dehydrogenase (LDH) was used as a model protein in both low concentrations to avoid self-stabilization and in high concentrations. The effect of different concentrations of Tween 80 on the protein protection during the freeze-thawing process in relation to ice surface was also evaluated.

Experimental MaterialsCited by: The endothermic transformation of a PEG-ice structure at −15°C in the heating process is strongly correlated to the protective ability of PEG in the freeze-thawing process of LDH. To obtain the highest protein activity after the freeze-thawing process, the formulation shall be transformed by a low cooling and heating rate.

Saccharides, including sucrose, trehalose, mannitol, and sorbitol, are commonly employed as stabilizers, cryoprotectants, and/or tonicity adjusters in protein formulations. During the thawing of a protein-containing formulated bulk drug substance conducted prior to a drug product (DP) filling operation, a white, crystalline precipitate was observed.

In addition, upon thawing, vial. Numerous studies have been attempted to understand and mitigate protein denaturation during freeze-thawing, and thereby provide guidelines for optimization of formulation and process.

Protein freeze-thawing is frequently used to stabilize and store recombinantly produced proteins after different unit operations in upstream and downstream processing. However, freeze-thawing is often accompanied by product damage and, hence, loss of product.

Different effects are responsible, including cold denaturation, aggregation effects, which are caused by inhomogeneities in protein. The science and the art of pharmaceutical formulation keeps evolving as new materials, methods, and machines become the process of ob-taining the information may be cumbersome, in which this is restricted to prototype formulations to keep the size of the book manageable and to reduce re-dundancy.

The purpose of the study was to investigate the protective mechanism of a non-ionic surfactant, Tw at freeze-thawing with controlled temperature history of a model protein, lactate.

Abstract. Freeze-thawing is a common unit operation during the production of protein-based therapeutics. Bulk protein solutions are often stored in frozen state for extended periods, and thawed to room temperature prior to downstream process operations including lyophilization, add-in formulation ingredients step, and fill and finish processes.

Formation of protein aggregates and subvisible particles during the manufacturing of drug products are a major concern due to the potential immunogenicity of protein aggregates in patients (17–22).

There have been studies to determine the impact of potential freeze-thaw factors on aggregation of proteins. The collapse temperature (Tc) and the glass transition temperature of freeze-concentrated solutions (Tg') as well as the crystallization behavior of excipients are important physicochemical characteristics which guide the cycle development in freeze-drying.

The most frequently used methods to determine these values are differential scanning calorimetry (DSC).

Bulk Freeze–Thawing of Macromolecules Effects of Cryoconcentration on Their Formulation and Stability. BioProcess Int. 5(6)44– 20 Miller R, et al. Dynamics of Protein and Mixed Protein/Surfactant Adsorption Layers at the Water–Fluid Interface. Adv. Colloid Interface Sci. 86(1) 39–   Freeze–thaw processes affect the quality of biopharmaceutical proteins (1–13) and human cells (14).It has been reported that no method consistently controls freezing and thawing rates for biological formulations (1).My recent study refutes that claim with validated rate-controlled freezing and thawing of such formulations in L single-use bags (15).

Given the great variety of techniques for analyzing and characterizing proteins (Chapter 2), it is a challenge to assess which of the assays are relevant to developing a stable formulation and delivery system, i.e., stability-indicating many of the chemical degradations in proteins are fairly well understood, particularly in regard to how conformation and primary.

The authors have identified an approach to stabilize PBS-based formulation for a monoclonal antibody (mAb). The effect of sodium chloride, nonionic surfactant, protein concentration, polyols, and freezing rates on freeze-thaw stability of a mAb was studied in 12 PBS-based formulations using six different freezing protocols.

Investigation of the stabilizing effects of hydroxyethyl cellulose on LDH during freeze drying and freeze thawing cycles. Pharmaceutical. A systematic investigation was performed to better understand the protein and solute distribution along with potential of aggregate formation during freeze and thaw process.

A significant solute and protein concentration gradient was observed for. Corpus ID: Freeze-thaw studies of a model protein, lactate dehydrogenase, in the presence of cryoprotectants. @article{NemaFreezethawSO, title={Freeze-thaw studies of a model protein, lactate dehydrogenase, in the presence of cryoprotectants.}, author={Saurabh Nema and Kenneth E.

Avis}, journal={Journal of parenteral science and technology: a. A mathematical model that simulates temperature profiles during freezing process of standard pharmaceutical formulations (mannitol and BSA based) was set up in two‐dimensional axsymmetric space, and the ice crystal mean sizes were semi empirically estimated from the resulting temperature profiles.By incorporating local chain stiffness in the protein model, a homopolymer can fold into a β-hairpin.

Computational Investigation of the Effect of Pressure on Protein Stability. A model-based approach for the rational design of the freeze-thawing of a protein-based formulation.

Pharmaceutical Development and Technology17,