Mechanism analysis of sulfobetaines' activity to prevent protein aggregation and application of sulfobetaines to unstable proteins

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Aggregation of proteins brings about severe problems in drug development. Although sulfobetaines have been known to prevent protein aggregation, its mechanisms have been elusive. Here we found that sulfobetaines accelerate inter-conformer exchange rates of proteins and increase flexibility of loops. In addition, sulfobetaines were found to make proteins unstable depending on the identity of proteins and buffer conditions. Prevention of protein aggregation by sulfobetaines did not correlate with enhancement of thermostability of proteins. Sulfobetaines were found to be useful for protecting antibodies and for efficient purification of unstable proteins.