Aggregation of Therapeutic Proteins - download pdf or read online

By Wei Wang, Christopher J. Roberts

ISBN-10: 0470411961

ISBN-13: 9780470411964

ISBN-10: 0470769823

ISBN-13: 9780470769829

This booklet supplies pharmaceutical scientists an up to date source on protein aggregation and its results, and to be had easy methods to keep watch over or decelerate the aggregation method. whereas major development has been made long ago decade, the present figuring out of protein aggregation and its effects remains to be immature. Prevention or maybe reasonable inhibition of protein aggregation has been regularly experimental. the information during this booklet can significantly aid pharmaceutical scientists within the improvement of healing proteins, and in addition instigate additional clinical investigations during this zone. This ebook fills one of these desire by means of supplying an summary at the factors, results, 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 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 methods 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 techniques to coping with Protein Aggregation in Product improvement (pages 333–365): Wei Wang and Nicholas W. Warne
Chapter nine Case experiences 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 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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1) Hydrophobicity and apolarity have been shown to be the primary factors that drive proteins to the condensed state because of the large heat capacity change associated with this process. The driving force for hydrophobic collapse is modulated by the temperature, pH, and dielectric constant (ε) of the solvent. At extremes of any condition, structural and dynamic changes are apparent. 42 The MG retains much of the secondary structure of the native state, but tertiary packing is disrupted such that the residues in the core are solvated efficiently.

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.

32 Although the exact structure of toxic species is unknown, these soluble aggregates all possess the ability to interact with and cross membranes and to disrupt ionic gradients. As such, it was proposed that beta barrels might form in the membrane, mimicking the structure of ion channels (Fig. 33 Amyloids have been induced to form in the presence of membranes, detergents, surfactants, polyanions, and compounds that change the dielectric of the solvent, which suggests that conformational changes mediate aggregation.

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


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