Abstract
Amyloids are a class of insoluble proteinaceous substances generally composed of linear un-branched fibrils that are formed from misfolded proteins. Conformational diseases such as Alzheimer's disease, transmissible spongiform encephalopathies, and familial amyloidosis are associated with the presence of amyloid aggregates in the affected tissues. The majority of the cases are sporadic, suggesting that several factors must contribute to the onset and progression of these disorders. Among them, in the past 10 years, non-enzymatic glycation of proteins has been reported to stimulate protein aggregation and amyloid deposition. In this review, we analyze the most recent advances in this field suggesting that the effects induced by glycation may not be generalized as strongly depending on the protein structure. Indeed, being a post-translational modification, glycation could differentially affects the aggregation process in promoting, accelerating and/or stabilizing on-pathway and off-pathway species.
Highlights
Amyloids are a class of insoluble proteinaceous substances generally composed of linear un-branched fibrils that are formed from misfolded proteins
The above referred considerations make the study of advanced glycation end-products (AGEs) one of the most important areas of biomedical research today
Regardless of the chronology of AGEs formation, it is known that its accumulation is related to sustained inflammatory responses and oxidative stress, which is a common feature in many neurodegenerative disorders
Summary
Amyloids are a class of insoluble proteinaceous substances generally composed of linear un-branched fibrils that are formed from misfolded proteins. The propensity of normally folded proteins to form amyloid-like fibrils increases in conditions that allow the protein to break the major unfolding energy barrier, favoring partial unfolding of the native state. PROTEIN GLYCATION AND AMYLOIDOSIS the aggregation process of amyloidogenic proteins has been widely studied in vitro and many physiological (environmental and genetic) factors involved have been identified, the molecular mechanisms underlying the formation of aggregates in vivo and in pathological conditions are still poorly understood.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
