By Wei Wang, Christopher J. Roberts
This publication supplies pharmaceutical scientists an up to date source on protein aggregation and its outcomes, and on hand ways to keep watch over or decelerate the aggregation technique. 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 regularly experimental. the data during this e-book can enormously support pharmaceutical scientists within the improvement of healing proteins, and in addition instigate additional medical investigations during this region. This booklet fills this kind of desire by means of delivering an outline at the explanations, outcomes, characterization, and keep watch over of the aggregation of healing proteins.Content:
Chapter 1 primary 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 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 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 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 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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Additional info for Aggregation of Therapeutic Proteins
A survey of protein structures revealed that beta sheets are often protected from intermolecular association in their native conformation because they are covered by helices. Alternatively, the newly uncoiled region may sample β-conformations more frequently and may directly participate in aggregation. If a competition exists between the two secondary structures in the same sequence, structural stabilization and conditions that favor helical organization would prevent aggregation. If the exposure of the existing beta structure is responsible for aggregation, then preservation of helicity in the absence of tertiary structure retention would be insufficient to prevent aggregation.
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. Although proteins with larger charged surface areas are often more soluble and it might be expected that water would be retained around charged moieties, it has already been noted that too high a charge density often produces disordered proteins, which have reduced retention of water at their surface.
When polar or charged residues occupy the remaining positions, the opposite face of the helix is amenable to interaction with water resulting in a soluble arrangement. Helices composed mostly of hydrophobic residues are poorly solvated and must be embedded in the core of a larger assembly. Beta sheets rely on the formation of hydrogen bonds between residues that are distant in the sequence. 65 This pattern generates compatible interactions between strands and produces the expanded hydrophobic surface necessary to sustain collapse as well as an apposed hydrophilic surface to support the solubility of the folded form.
Aggregation of Therapeutic Proteins by Wei Wang, Christopher J. Roberts