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

By Wei Wang, Christopher J. Roberts

This ebook offers pharmaceutical scientists an up to date source on protein aggregation and its results, and on hand the right way to keep an eye on or decelerate the aggregation method. whereas major development has been made long ago decade, the present knowing of protein aggregation and its outcomes remains to be immature. Prevention or maybe average inhibition of protein aggregation has been in most cases experimental. the information during this booklet can significantly aid pharmaceutical scientists within the improvement of healing proteins, and in addition instigate extra clinical investigations during this quarter. This publication fills this sort of want by way of supplying an outline at the motives, effects, 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 impression of Aggregation?Prone areas in Proteins and healing Monoclonal Antibodies (pages 103–118): Sandeep Kumar, Xiaoling Wang and Satish okay. 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 ways to manage Protein Aggregation in the course of Bulk creation (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 coping with Protein Aggregation in Product improvement (pages 333–365): Wei Wang and Nicholas W. Warne
Chapter nine Case reviews 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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7 in solution but can be perturbed substantially in the context of a folded protein due to the local microenvironment. His participates in hydrogen bonding, where it can act as a donor or as an acceptor. 57–59 The uncharged species is easily accommodated in the hydrophobic core because it can add stability through hydrophobic and aromatic interactions as well. Electrostatic interactions involving Asp, Glu, Lys, and Arg are also observed in the core of folded proteins in the form of salt bridges.

Model of macroscopic fibril structure composed of four sheets shown looking down the long axis (A) and from the side, showing the twist (B). From Reference 26. 4. Peptide fragments arrange in beta barrel formations during simulations. Closed or open barrels result from different peptide sequences. Reproduced with permission from Reference 33. 22 Their diameters vary, but often it has been shown that a discrete number of protein molecules are involved, suggesting that specific structural contacts are made between each polypeptide chain.

Closed barrels convert to orthogonal sheets, while open barrels generate parallel sheets. This finding suggests that different proteins may undergo semi-common intermediate aggregation states that lead to distinctly different final morphologies. 30 Higher-resolution structural information about each of these systems is needed to investigate the β-barrel hypothesis and to better understand the relationship between aggregate structure and membrane permeability. Most proteins unfold as the temperature is elevated, and at temperatures below their unfolding transition (Tm), where only partial unfolding is observed, aggregates begin to form.

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