Dissolution of protein aggregation by small amine compounds

Proteins tend to form insoluble and inactive aggregation when they are exposed to extreme-environment such as high temperature. One of the major approaches for a new method to prevent undesirable aggregation formation is to explore new small molecular additives, such as ion, amino acid, and small amount of organic solvent and denaturant. Here we propose that polyamines, which is naturally occurring amine compounds, exhibited much stronger preventive effect on heat-induced protein aggregation formation than arginine, the most conventionally used additive. In addition, spermidine could even dissolve protein fibril, although the fibrils are resistant against glycine and arginine. These results implied that polyamines could function as a new class for aggregation suppressors to stabilize heat-labile proteins. Moreover, polyaminies might be important precursors for drugs against folding-related diseases.