By Wei Wang, Christopher J. Roberts

ISBN-10: 0470411961

ISBN-13: 9780470411964

ISBN-10: 0470769823

ISBN-13: 9780470769829

This e-book offers pharmaceutical scientists an updated source on protein aggregation and its effects, and to be had tips on how to keep an eye on or decelerate the aggregation strategy. whereas major development has been made long ago decade, the present knowing of protein aggregation and its outcomes continues to be immature. Prevention or maybe average inhibition of protein aggregation has been in most cases experimental. the information during this e-book can enormously support pharmaceutical scientists within the improvement of healing proteins, and in addition instigate additional clinical investigations during this zone. This e-book fills any such desire through delivering an summary at the factors, 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 impression 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 ways to regulate 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 handling Protein Aggregation in Product improvement (pages 333–365): Wei Wang and Nicholas W. Warne
Chapter nine Case reports 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 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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With respect to this idea, partial unfolding of a protein may lead to increased exposure of regions that retain such structural features, and these foldon-like segments may then nucleate intermolecular assembly. The diffusion–collision (DC) model presented by Karplus and Weaver is based on the formation of microdomains within the protein structure, such as transiently stable helices. 128 In most applications of this model, only native collision–coalescence events are permitted. 129 DC and foldons share the common idea that preformed structural elements or tendencies are encoded in the sequence, but DC differs from the foldon concept in that folding need not be fully cooperative and is quantified using a molecular modeling approach.

41,50 Aromatic residues (Phe, Trp, and Tyr) contribute to hydrophobic interactions that stabilize the core because they have relatively large apolar surface areas. 51 Moreover, the stacked orientation is an efficient packing arrangement. 54 Pi bonds produce a dipole, which also enables favorable interaction with cations. There are many examples of structures in which Lys and Arg side chains are found to interact with aromatic rings in folded proteins. 56 Charged residues, including Glu and Asp (acidic) and Lys and Arg (basic) most often appear on the surface of folded proteins.

Instead, the barrier to structural rearrangement is minimal and assembly occurs as a consequence of frequent conversion to the aggregation-prone conformation. The rate of formation of aggregates increases with increasing concentration of protein in this model because the probability of productive collisions increases. 2 AGGREGATION OF THERAPEUTIC PROTEINS Oligomeric Intermediates The nucleation–polymerization (NP) model was developed to account for the lag phase preceding the growth of insoluble fibers from untainted protein samples.

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