Aggregation of Therapeutic Proteins by Wei Wang, Christopher J. Roberts

By Wei Wang, Christopher J. Roberts

This e-book provides pharmaceutical scientists an up to date source on protein aggregation and its outcomes, and on hand ways to regulate or decelerate the aggregation technique. whereas major development has been made long ago decade, the present realizing of protein aggregation and its outcomes remains to be immature. Prevention or perhaps average inhibition of protein aggregation has been in most cases experimental. the data during this publication can enormously aid pharmaceutical scientists within the improvement of healing proteins, and in addition instigate extra medical investigations during this region. This publication fills this sort of desire by means of offering an summary at the motives, effects, characterization, and regulate of the aggregation of healing proteins.Content:
Chapter 1 basic 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 ok. 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 techniques to manage 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 reviews 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 viewpoint 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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Partial unfolding permits the association of monomers through exposure of previously inaccessible residues. 63 In many proteins, it is apparent that the appropriate conditions for aggregation are met in partially unfolded states, but experimental requirements do not permit determination of whether aggregation proceeds solely from a partially unfolded state or whether the fully unfolded form also aggregates rapidly. In some cases, however, completely unfolded forms of proteins do not appear to aggregate.

106,107 Based on residence time, little associated water is detected in unfolded proteins. This data suggest that the water molecules may be organized into a more structured network around the protein. This hydration shell is thought to promote stability in part because the water binds more tightly to the folded protein than does bulk water to the unfolded form, a simple mass action effect. The basis for increased residence time has not been quantitatively established as of yet and does not appear to correlate with solubility.

What remains to be explained is the selective basis for and the mechanisms by which a polypeptide achieves the native fold or an aggregate-prone intermediate conformation. While coordinated unfolding at specific sequences and association is required to generate fibrillar aggregates, amorphous aggregation may arise from heterogeneity among the unfolded population in which associations between several states have approximately equal free energies. This could permit an irregular macroscopic organization to develop as a result of intermolecular interaction at multiple sites.

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