By Wei Wang, Christopher J. Roberts
This publication provides pharmaceutical scientists an updated source on protein aggregation and its results, and on hand easy methods to regulate or decelerate the aggregation procedure. whereas major development has been made long ago decade, the present figuring out 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 ebook can enormously support pharmaceutical scientists within the improvement of healing proteins, and in addition instigate extra clinical investigations during this quarter. This publication fills this kind of desire by means of offering an outline at the motives, results, characterization, and keep watch over of the aggregation of healing proteins.Content:
Chapter 1 primary buildings 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 identity and influence of Aggregation?Prone areas in Proteins and healing Monoclonal Antibodies (pages 103–118): Sandeep Kumar, Xiaoling Wang and Satish okay. Singh
Chapter four exterior elements 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 ok. Sharma and Devendra S. Kalonia
Chapter 6 ways 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 ways to handling Protein Aggregation in Product improvement (pages 333–365): Wei Wang and Nicholas W. Warne
Chapter nine Case stories regarding 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 point of view 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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Extra info for Aggregation of Therapeutic Proteins
Folding must be completely cooperative to fit this model. Indeed, many early observations made concerning protein folding and unfolding obeyed such two-state kinetics. These early studies were almost all performed on small globular proteins that fold cooperatively, and the results show that this model describes folding well for this type of protein, at least to a first approximation. Because the timescale for folding is often on the order of milliseconds, only the unfolded and native states were observed in equilibrium experiments, validating the model.
6. Domain-swapped dimer structure of cystatin C. The fold of chicken cystatin (PDB entry 1CEW), defining the topology of this class of proteins (top). Domainswapped dimer of HCC in a view similar to (middle) and in a perpendicular orientation (bottom) emphasizing the beta sheet in the domain switch region (open interface) and the site of the L68Q mutation (red dot). From Reference 64. See color insert. vented domain swapping, and greatly diminished amyloid fibril formation, indicating the domain-swapped dimer is an intermediate that propagates aggregation.
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. These observations provided the foundation for the idea that the amino 12 AGGREGATION OF THERAPEUTIC PROTEINS acid sequence encodes structural information that influences folding and stability.