By Byeong S. Chang, Susan Hershenson (auth.), John F. Carpenter, Mark C. Manning (eds.)
Recombinant proteins and polypeptides stay an important category of biotechnology-derived brokers in state-of-the-art pharmaceutical undefined. over the last few years, our basic knowing of ways proteins degrade and the way stabilizing brokers paintings has made it attainable to process formula of protein prescription drugs from a way more rational aspect of view.
This booklet describes the present point of realizing of protein instability and the thoughts for stabilizing proteins below quite a few annoying stipulations.
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Additional info for Rational Design of Stable Protein Formulations: Theory and Practice
Guidance for Industry: Changes to an Approved Application: Specified Biotechnology and Specified Synthetic Biological Products; July 1997. J. , 1992a. Stability of protein pharmaceuticals, Part A: Chemical and physical pathways of protein degradation. Pharm. Biotech. Ser. Volume 2. Y. J. , 1992b. Stability of protein pharmaceuticals, Part B: In vivo pathways of degradation and strategies for protein stabilization. Pharm. Biotech. Ser. Volume 3. Y. P', 1993. Factors affecting shortterm and long-term stabilities of proteins.
Volume 3. Y. P', 1993. Factors affecting shortterm and long-term stabilities of proteins. Adv. Drug Delivery Rev. 10: 1. , 1991. Use of 2hydroxypropyl-beta-cyclodextrin as a solubilizing and stabilizing excipient for protein drugs. Pharm. Res. 8:792. , 1993. The development of stable protein formulations-A close look at protein aggregation, dearnidation and oxidation. Crit. Rev. Ther. Drug 11 :60. , 1992. Formulation concerns of protein drugs. Drug Dev. Ind. Pharmacy, 18:1311. , 1998. Preparation and characterization of a cocrystalline suspension of [Lys(B28),Pro(B29)] human insulin analogue.
Tiansheng Li and Linda O. Narhi • Amgen, Inc. Thousand Oaks, CA 91320. Rational Design of Stable Protein Formulations, edited by Carpenter and Manning. Kluwer Academic / Plenum Publishers, New York, 2002. 27 28 Tsutomu Arakawa et al. required during the refolding process. Expressed proteins located in the soluble fraction of the bacteria usually are those that contain no disulfide bonds in the native state. However, there are some exceptions to this rule. Even disulfidecontaining proteins can be expressed in the folded conformation or in a soluble, but misfolded, conformation.