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

By Wei Wang, Christopher J. Roberts

This ebook offers pharmaceutical scientists an updated source on protein aggregation and its effects, and on hand how you can keep an eye on or decelerate the aggregation procedure. whereas major growth has been made some time past decade, the present knowing of protein aggregation and its effects remains to be immature. Prevention or maybe reasonable inhibition of protein aggregation has been often experimental. the data during this booklet can enormously aid pharmaceutical scientists within the improvement of healing proteins, and in addition instigate additional clinical investigations during this quarter. This booklet fills this kind of desire via delivering an outline at the explanations, effects, characterization, and keep watch over 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 id and effect 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 okay. 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 methods to dealing with Protein Aggregation in Product improvement (pages 333–365): Wei Wang and Nicholas W. Warne
Chapter nine Case reviews concerning 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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Example text

These simple systems have obvious utility for investigating fundamental influences on protein folding, and the findings are relevant to protein aggregation. The fundamental parameters that influence the behavior of proteins in solution and the models that have been developed to explain their behavior are discussed below. 35,41 From a thermodynamic perspective, FUNDAMENTAL STRUCTURES AND BEHAVIORS OF PROTEINS 13 collapse of the polypeptide chain is an organizing event and also requires that water be removed from parts of the protein that form the core of the folded species.

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.

Addition of increasing amounts of reducing agent revealed an equilibrium between two dimeric forms, only one of which was able to form fibrils, suggesting that a conformational change in the domain-swapped dimer precedes fibril growth (Fig. 7. Schematic model for the fibril formation of T7EI L19C/S95C, illustrating the need for a structural transition from the dimeric state to generate the fibrillar arrangement. Each subunit is colored either in light or dark gray. Black dots represent disulfide bonds, and SH represents free cysteine.

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