By Wei Wang, Christopher J. Roberts
This booklet provides pharmaceutical scientists an up to date source on protein aggregation and its results, and to be had how you can regulate or decelerate the aggregation method. whereas major development has been made some time past decade, the present knowing of protein aggregation and its results remains to be immature. Prevention or perhaps reasonable inhibition of protein aggregation has been more often than not experimental. the data during this publication can drastically support pharmaceutical scientists within the improvement of healing proteins, and in addition instigate extra medical investigations during this zone. This ebook fills the sort of desire through delivering an summary at the reasons, results, characterization, and keep watch over of the aggregation of healing proteins.Content:
Chapter 1 basic constructions and Behaviors of Proteins (pages 1–61): Jennifer S. Laurence and C. Russell Middaugh
Chapter 2 Protein Aggregation Pathways, Kinetics, and Thermodynamics (pages 63–102): Yi Li and Christopher J. Roberts
Chapter three id and effect of Aggregation?Prone areas in Proteins and healing Monoclonal Antibodies (pages 103–118): Sandeep Kumar, Xiaoling Wang and Satish ok. Singh
Chapter four exterior components Affecting Protein Aggregation (pages 119–204): Wei Wang, Ning Li and Stan Speaker
Chapter five Experimental Detection and Characterization of Protein Aggregates (pages 205–256): Vikas okay. Sharma and Devendra S. Kalonia
Chapter 6 methods to regulate Protein Aggregation in the course of Bulk construction (pages 257–299): Linda O. Narhi, Yijia Jiang, Rohini Deshpande, Sohye Kang and Joseph Shultz
Chapter 7 Protein Aggregation and Particle Formation: results of formula, Interfaces, and Drug Product production Operations (pages 301–331): Hanns?Christian Mahler, Stefan Fischer, Theodore W. Randolph and John F. Carpenter
Chapter eight methods to dealing with Protein Aggregation in Product improvement (pages 333–365): Wei Wang and Nicholas W. Warne
Chapter nine Case stories related to Protein Aggregation (pages 367–401): Rahul S. Rajan, Tiansheng Li and Tsutomu Arakawa
Chapter 10 Aggregation and Immunogenicity of healing Proteins (pages 403–433): Vasco Filipe, Andrea Hawe, Huub Schellekens and Wim Jiskoot
Chapter eleven Regulatory standpoint on Aggregates as a Product caliber characteristic (pages 435–451): Wendy C. Weinberg, Linan Ha, Susan L. Kirshner and Daniela I. Verthelyi
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Additional info for Aggregation of Therapeutic Proteins
Salt bridge formation on the surface of a protein can improve structural stability by contributing a favorable tertiary interaction between nonsequential residues. 92 If the interaction alters the tertiary structure, aggregation may be irreversible as a result of more extensive structural rearrangement. Although most of the protein core is composed of hydrophobic moieties, structures in the Protein Data Bank (PDB) show that acidic and basic side chains are often buried in the protein core. The proteins exist in stable folded structures as long as the charge is offset in a way that its presence is more stabilizing than destabilizing.
The microdomains arise from fundamental features of the sequence, and the collision between domains depends on the distances separating the domains. With this approach, mutations can be introduced to assess easily the effect on folding rate and the formation of intermediates. A similar concept may play a role in the aggregation of proteins, in which aggregation “hot spots” are unveiled as a protein unfolds. Peptide sequences derived from proteins that aggregate are prone to rapid assembly when examined in the absence of the full, folded sequence.
38 Since experimental results show that proteins achieve native folds in ms-sec rather than the predicted expanses of years, the hypothesis emerged that folding must be directed in some way toward the native state. Since then, many have worked to identify and explain the parameters that permit rapid folding of proteins to their native state. Proteins having different amino acid sequences have different rates of folding and unfolding as well as differing stabilities. Single amino acid substitutions in a protein can dramatically affect these processes.