SDS modulates amyloid fibril formation and conformational change in succinyl-ConA at low pH.

The anionic surfactant sodium dodecyl sulfate (SDS) is homologous to the cellular membrane lipids, and is known to stimulate amyloid fibrillation in several proteins. However, the mechanism by which SDS influences aggregation and structural changes in succinylated protein has not been determined. In this study, we observed the effects of variable SDS concentrations on succinyl-ConA aggregation at pH 3.5 and proposed a possible mechanism of SDS-induced succinyl-ConA aggregation. We used several biophysical techniques to identify the changes caused by SDS. Our results suggest that SDS stimulates succinyl-ConA aggregation in a concentration-dependent manner. From turbidity measurements, it was evident that a very low concentration (<0.1 mM) of SDS did not induce succinyl-ConA aggregation and proteins remained soluble. However, aggregations were observed at 0.1-2.5 mM SDS, which then dissipated at SDS concentrations above 2.5 mM. Far-UV CD results suggest that the β-sheet secondary structure of succinyl-ConA transformed into the cross-β-sheet structure in the presence of aggregating SDS concentrations. Notably, at SDS concentrations above 2.5 mM, the succinyl-ConA β-sheet transformed into an α-helical structure. The SDS-induced succinyl-ConA amyloid-like aggregates were confirmed by transmission electron microscopy (TEM). We propose that SDS modulates amyloid fibrillation in succinyl-ConA due to electrostatic and hydrophobic interactions and succinylation affects SDS-induced succinyl-ConA aggregation.