pH-dependent stability and conformation of the recombinant human prion protein PrP(90-231)

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Abstract

A recombinant protein corresponding to the human prion protein domain encompassing residues 90-231 (huPrP(90-231)) was expressed in Escherichia coli in a soluble form and purified to homogeneity. Spectroscopic data indicate that the conformational properties and the folding pathway of huPrP(90-231) are strongly pH-dependent. Acidic pH induces a dramatic increase in the exposure of hydrophobic patches on the surface of the protein. At pH between 7 and 5, the unfolding of hPrP(90-231) in guanidine hydrochloride occurs as a two-state transition. This contrasts with the unfolding curves at lower pH values, which indicate a three-state transition, with the presence of a stable protein folding intermediate. While the secondary structure of the native huPrP(90-231) is largely α-helical, the stable intermediate is rich in β-sheet structure. These findings have important implications for understanding the initial events on the pathway toward the conversion of the normal into the pathological forms of prion protein.

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Swietnicki, W., Petersen, R., Gambetti, P., & Surewicz, W. K. (1997). pH-dependent stability and conformation of the recombinant human prion protein PrP(90-231). Journal of Biological Chemistry, 272(44), 27517–27520. https://doi.org/10.1074/jbc.272.44.27517

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