2025 Volume 74 Issue 7 Pages 599-612
Protein misfolding and aggregation play crucial roles in several neurodegenerative disorders. In this study, sulfobetaine-10 (SB10) has been demonstrated to stabilize proteins and inhibit aggregation by preserving solubility and retaining native-like structures when exposed to reducing agents such as DTT. We have measured changes in turbidity, secondary, tertiary structures, and ThT fluorescence. When SB10 concentration was used above the critical micelle concentration (CMC), it successfully stops hen egg white lysozyme (HEWL) aggregation. Below CMC, SB10 induces aggregation in the DTT reduced HEWL. However, it does not cause aggregated proteins to regain their native structure. SB10’s zwitterionic composition restricts its capacity to aid in protein refolding, highlighting the significance of electrostatic interactions in this process. This research indicates that SB10 has promise in therapeutic protein formulations and as a remedy for protein misfolding diseases.
