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

By Wei Wang, Christopher J. Roberts

This booklet offers pharmaceutical scientists an updated source on protein aggregation and its results, and to be had the way to keep an eye on or decelerate the aggregation technique. whereas major growth has been made some time past decade, the present figuring out of protein aggregation and its effects continues to be immature. Prevention or perhaps reasonable inhibition of protein aggregation has been in general experimental. the information during this booklet can vastly aid pharmaceutical scientists within the improvement of healing proteins, and in addition instigate extra clinical investigations during this quarter. This e-book fills any such want through supplying an summary at the reasons, effects, characterization, and regulate 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 influence 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 methods to regulate 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 stories 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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Extra resources for Aggregation of Therapeutic Proteins

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The disparities between the models suggest that differences in sequence, which affect side-chain packing, may be responsible for the morphological differences observed in aggregates. The phenomenon of aggregation is complex and seems to involve a series of intermediate structural states, some of which may be amorphous, along the path toward forming highly ordered fibrillar amyloid structures (Fig. 9 Some of these states have been described in varying degrees of detail. Many plaque-forming proteins undergo an early transition from native monomers to oligomeric aggregates before fibrils are detected.

1 Monomer Conversion Templated assembly (TA) was proposed soon after the discovery of prion proteins to explain their mechanism of infectivity. 120 A favorable energy difference driving α′ to α is proposed, but the barrier to conversion would be large for the wild-type protein under normal physiological conditions. This makes formation of the dimer highly improbable. The existence of α2, however, would then lower the energy barrier for a subsequent conformational rearrangement of α′, allowing α2 to act as a template for propagation.

Secondarily, dihedral angles are affected by steric restrictions that the side chain imposes on the backbone. 69–71 The degree to which this bias exists depends on the amino acid and on the sequence in which it is embedded. Polyalanine sequences have a strong tendency to form alpha helices. Leu is found approximately 60% of the time in helices and 25% of the time in beta strands, whereas beta-branched amino acids (Val, Ile) tend to adopt an extended beta structure, such that Ile is located in beta strands in about 75% of sequences.

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