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7439367 
Journal Article 
Protein Aggregation, Related Pathologies, and Aging 
Kar, K; Anand, BG; Dubey, K; Shekhawat, DS; , 
2020 
Springer Singapore 
Singapore 
Models, Molecules and Mechanisms in Biogerontology 
419-441 
Self-assembly of protein molecules into higher order structures is a fundamental process in biology, which has a direct relevance to many metabolic processes in life. Though self-assembly of various structural proteins such as collagens and laminins is vital to both structural and functional properties of several tissue components and scaffolds, self-assembly of soluble proteins and peptides leading to formation of cross-β-structured amyloid aggregates, on the contrary, has been linked to many lethal diseases. Since proteins are considered as important biomacromolecules which are directly or indirectly involved in almost every metabolic process, the occurrence of protein aggregation is predicted to influence the normal physiology of living beings. The onset of protein aggregation into amyloid fibrils has been linked to more than ~45 pathologies, including a series of neurodegenerative disorders such as Aβ-linked Alzheimer’s disease, huntingtin-linked Huntington’s disease, and α-synuclein-linked Parkinson’s disease. These neurodegenerative diseases are known as progressive disorders in which the lethality rises with the increase in the age of the individuals. Hence, the question of what influence the alternations in the age-linked metabolic processes have on the process of protein aggregation becomes very significant. In this chapter, we have attempted to discuss selected research reports on fundamental understanding of the process of protein aggregation and its biological relevance, particularly exploring the vital link between aging and amyloid-related pathologies.