Abstract
Prevention of aggregation is critical for analyzing protein structure. Non-detergent sulfobetaines (NDSBs) are known to prevent protein aggregation, but the molecular mechanisms of their anti-aggregation effect are poorly understood. To elucidate the underlying mechanisms, we analyzed the effects of dimethylethylammonium propane sulfonate (NDSB-195) on acidic fibroblast growth factor (aFGF). NDSB-195 (0.5 M) increased both aggregation and denaturation temperatures of aFGF by 4 °C. Chemical shift perturbation analyses indicated that many affected residues were located at the junction between a β-strand (or 3 10-helix) and a loop, irrespective of the chemical properties of the residue. The apparent dissociation constants of the interaction ranged from 0.04 to 3 M, indicating weak interactions between NDSB and protein molecules.
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