Biotechnological pharmaceuticals protein stability

Yamamoto, O. (1992), Effect of radiation on protein stability, in Ahern,T. J., and Manning, M. C. Eds., Pharmaceutical Biotechnology, Vol. 2, Stability of Protein Pharmaceuticals. Part A Chemical and Physical Pathways of Protein Degradation, Plenum, New York. 

Costantino, H. R., Langer, R., and Klibanov, A. (1995), Aggregation of a lyophilized pharmaceutical protein, recombinant human albumin effect of moisture and stabilization excipients, BioTechnology, 13,493-496. 

Y. J. Wang and R. Pearlman, Stability and Characterization of Protein and Peptide Drugs Case Histories, Plenum Press, New York, Pharmaceutical Biotechnology, Volume 5, 1993. 

The advent of biotechnology, bioengineering and pharmaceutical delivery systems has increased the requirements for solubility and stability of macromolecules under a variety of versatile and unique conditions and subsequently the use of non-aqueous solvents. Specihc applications include a) isolation, purification, precipitation and crystallization of biopharmaceuticals, b) processing methods such as spray drying and microencapsulation, and c) formulation of proteins for delivery systems requiring high concentrations and prolonged stability, such as implants and depots. 

The stability of biotechnology-produced products, proteins (macromolecules), and peptides is unique when compared with conventional pharmaceuticals (small molecules). Protein degradation by both chemical and physical processes leads to the loss of biological activity, whereas peptides decompose only through chemical instability with loss of efficacy and produce undesirable biological effects. 

Pearlman, R.nnd Wang, Y.J. (1996) Formulation, characterization, and stability of protein drugs. Case Histories. In Bortchardt, R.T. (ed.). Pharmaceutical Biotechnology. Plenum Press, New York. 

Modern calorimetry has transformed and advanced to such a degree that today its acute sensitivity and flexibility has made it an indispensable tool throughout the life sciences. Ultrasensitive calorimetry now plays an integral role in biotechnology, providing researchers with essential information on the thermodynamics, structure, stability, and functionality of proteins, nucleic acids, lipids, and other biomolecules. Ultrasensitive calorimetry is a vital tool for R D in pharmaceuticals, genetics, energy, and materials—in almost any area where the measurement and controlled manipulation of substances and interactions are required at the molecular level. 

S Li, C Schoneich, R Borchardt. Chemical instability of protein pharmaceuticals mechanisms of oxidation and strategies for stabilization. Biotechnology and Bioengineering 48 490-500, 1995. 

Flow reactors of aU shapes, sizes, and uses are encountered in aU phases of fife. Examples of interest to bioengineers include the pharmaceutical industry, to produce aspirin, penicfifin, and other drugs the biomass processing industry, to produce alcohol, enzymes and other specialty proteins, and value added products and the biotechnologically important tissue and cell culture systems. The type of reactor used depends on the specific application and on the scale desired. The choice is based on a number of factors. The primary ones are the reaction rate (or other rate-limiting process), the product distribution specifications, and the catalyst or other material characteristics, such as chemical and physical stability. 

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