By Wei Wang, Christopher J. Roberts
This booklet offers pharmaceutical scientists an updated source on protein aggregation and its effects, and to be had the right way to regulate or decelerate the aggregation strategy. whereas major growth has been made long ago decade, the present figuring out of protein aggregation and its results continues to be immature. Prevention or maybe average inhibition of protein aggregation has been in general experimental. the information during this e-book can significantly support pharmaceutical scientists within the improvement of healing proteins, and in addition instigate extra medical investigations during this region. This e-book fills this type of desire through delivering an outline at the motives, outcomes, 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 identity 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 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 dealing with Protein Aggregation in Product improvement (pages 333–365): Wei Wang and Nicholas W. Warne
Chapter nine Case experiences 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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Additional info for Aggregation of Therapeutic Proteins
Thermophilic organisms are adapted to function at greatly elevated temperatures, and their proteins can occasionally resist thermal unfolding above 100°C. A computational study comparing the stability of thermophilic and mesophilic proteins showed that the enhanced stability of the former was imparted by surface residues. 83 Proteins from thermophiles were noted to display higher percentages of Lys, Arg, and Glu and lower fractions of Ala, Asp, Asn, Gln, Thr, Ser, and His on their solvent-accessible surface than mesophiles.
This difference in kinetics may provide an explanation for why alpha to beta conversion is observed in aggregation. When alpha helices are destabilized, beta strands that exist may become amenable to rapid intermolecular association since they are no longer protected by intramolecular structural elements. 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.
3). Earlier models are similar in many regards. 2. Molecular model of cross-beta structure showing interdigitation of side chains that form the tight packing arrangement in the islet amyloid polypeptide (IAPP) sequence NNFGAIL (A) and the backbone hydrogen bonding between strands (B). See color insert. model to include the NMR-based side-chain interactions resulted in poorer alignment between the sheets. The common element of the cross-β arrangement among unrelated sequences indicates that a backbone conformation amenable to beta structure and compatible interaction between side chains in the strands stabilize fibrillar aggregates.