Document Type: Short Review Article

Author

Master of cellular and molecular science/biochemistry field of study, Islamic Azad University (IAU), Science and Research Branch, Sanandaj, Iran.

Abstract

Diseases resulting from protein accumulations can be described mainly by improper folding and aggregation of endogenous proteins in affected tissues such as the brain or the heart. During misfolding and aggregation, the affected protein often loses its normal function, becomes more resistant to degradation, and often acquires toxic functions that can cause organ damage. Proteins generally require specific three-dimensional conformations in order to be soluble and function correctly in the body. Under stress conditions, normally soluble proteins can undergo structural changes and self-assembly, leading to their aggregation into insoluble deposits, referred to as amyloids. Amyloids from different proteins share several structural properties: they all have a fibrillar morphology and cross-β structure, whereby intermolecular main-chain hydrogen bonding acts as one primary stabilizing interaction. In conclusion, protein aggregation is the process by which misfolded proteins adopt a conformation that causes its polymerization into aggregates and organized fibrils. Many neurodegenerative diseases (amyloidoses) are associated with protein aggregation, though smaller oligomeric forms of the misfolded (amyloidogenic) proteins have been implicated as the causative agent. This study investigates those factors involved in disease and abnormalities arising from protein aggregation one by one. Also, it can be reviewed as a comprehensive glance for the process of protein aggregation whether from a structural or clinical point of view.

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