High hydrostatic pressure can induce partially unfolded protein conformations that are highly aggregation prone under conditions that normally favour the native state. We investigated the pressure stability of insulin at pH 2 with Fourier transform infrared spectroscopy. We do not observe any cooperative change up to 13 kbar. All spectral changes in the amide I area are fully reversible and are assumed to arise from the elastic effect of pressure, which causes no conformational changes. Moreover, insulin has no higher temperature-induced aggregation tendency when pressure pre-treated.
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