Download e-book for iPad: Aggregation of Therapeutic Proteins by Wei Wang, Christopher J. Roberts

By Wei Wang, Christopher J. Roberts

ISBN-10: 0470411961

ISBN-13: 9780470411964

ISBN-10: 0470769823

ISBN-13: 9780470769829

This booklet supplies pharmaceutical scientists an updated source on protein aggregation and its outcomes, and on hand the way to keep an eye on or decelerate the aggregation technique. whereas major development has been made some time past decade, the present figuring out of protein aggregation and its results continues to be immature. Prevention or perhaps reasonable inhibition of protein aggregation has been in general experimental. the data during this publication can tremendously aid pharmaceutical scientists within the improvement of healing proteins, and likewise instigate extra medical investigations during this region. This e-book fills this type of desire by way of supplying an summary at the motives, outcomes, 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 effect of Aggregation?Prone areas in Proteins and healing Monoclonal Antibodies (pages 103–118): Sandeep Kumar, Xiaoling Wang and Satish ok. 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 ok. Sharma and Devendra S. Kalonia
Chapter 6 techniques to manage 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 techniques 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 viewpoint 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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The major factors that have been shown to play a role in the specificity and stability of protein folds are derived from the chemical attributes of the amino acid sequence, including hydrophobicity, aromatic stacking, electrostatic interactions, steric constraints, and hydrogen bonding (secondary structure), as well as the efficiency of packing in the core and surface properties of the folded molecule. The contributions of each component to protein folding and stability are discussed below. ∆G = ∆H − T∆S.

111 Conversely, many native proteins are dramatically stabilized by the presence of polyanionic compounds,44,112–115 suggesting that specific knowledge of the mechanisms by which each event occurs is needed to explain the differing results. One possible mechanism of aggregation is that binding may induce and stabilize conformational changes that expose the apolar surface area. 63 When binding leads to stabilization of a protein, the conformation would be such that the accessible hydrophobic surface area is limited or it persists in a conformation that is not amenable to self-association.

7. 97,99 Groupings of charged residues on the surface of a protein can also influence the net charge by perturbing the pKa of residues in close proximity, but this usually has only a small effect, inducing fractional changes in the measured pKa. Structures of Aβ fibrils align such that strings of Glu residues are positioned adjacent to each other along the long axis of the fiber. The Glu side chains are surrounded by a high density of hydrophobic moieties on both sides. The high degree of hydrophobicity and close proximity of like charges both should contribute to elevating the pKa of the carboxylate group, lowering the barrier to association between sheets.

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


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