Amyloid-forming proteins are implicated in over 30 human diseases. The proteins involved in each disease have unrelated sequences and dissimilar native structures, but they all undergo conformational alterations to form fibrillar polymers. The fibrillar assemblies accumulate progressively into disease-specific lesions in vivo. Substantial evidence suggests these lesions are the end state of aberrant protein folding whereas the actual disease-causing culprits likely are soluble, non-fibrillar assemblies preceding the aggregates.

This book provides a comprehensive overview of the development of metabolic syndrome, the underlying mechanisms and therapeutic strategies for drug development. The authors examine the context of underlying molecular pathways and integrated physiology, then expanding the discussion to diseases associated with metabolic syndrome. The development of drug therapies for these diseases and complications is extensively covered. The book offers a comprehensive and in-depth view of energy metabolism, metabolic tissues and pathways, molecular mechanism-based drug discovery and clinical implications.