Although the aggregation process of amyloidogenic proteins has been widely studied in vitro and many physiological factors have been identified, the molecular mechanisms underlying the formation of aggregates in vivo and under pathological conditions are still poorly understood. Post‐translational modifications are known to affect protein structure and function. Some of these modifications might affect proteins in detrimental ways and lead to their misfolding and accumulation. Reducing sugars play an important role in modifying proteins, forming advanced glycation end‐products (AGEs) in a nonenzymatic process, called glycation. Recently, much attention has been devoted to the role played by glycation in stimulating amyloid aggregation and cellular toxicity. Proteins in amyloid deposits are often found glycated, suggesting a direct correlation between protein glycation and amyloidosis.
Part of the book: Exploring New Findings on Amyloidosis