Mesoscopic Properties And Molecular Mechanisms Of Iapp Amyloid Inhibition And Remodeling With Small Molecules

The amyloid aggregation of proteins is associated with a number of neurodegenerative diseases such like Alzheimeru0027s, Huntingtonu0027s and Parkinsonu0027s diseases, and also type-2 diabetes (T2D). Despite the physical and structural properties of the aggregating proteins, the corresponding amyloid aggregates feature some common characteristics including the formation of cross-β architecture and cytotoxicity to human cells, suggesting a common amyloid mechanism. Experimental studies have shown that several naturally-occurring small molecules, such as epigallocatechin gallate (EGCG), have an inhibitory effect on the aggregation of a wide range of those amyloid proteins, including islet amyloid polypeptide (IAPP, a.k.a.