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

Abstract 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 (