Journal
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
Volume 37, Issue 7, Pages 1127-1132Publisher
SPRINGER
DOI: 10.1007/s00249-008-0277-0
Keywords
high pressure; human serum albumin; misfolding; aggregation; conformational disease; infrared; spectroscopy
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Pressure unfolding-refolding and the subsequent aggregation of human serum albumin (HSA) was investigated by high-pressure Fourier transform infrared measurements. HSA is completely unfolded at 1 GPa pressure, but the unfolding is not cooperative. Hydrogen-deuterium exchange experiments suggest that a molten globule-like conformation is adopted above 0.4 GPa. An intermediate was formed after decompression, which differs from the native state only slightly in terms of the secondary structure, but this intermediate is more stable against the temperature-induced gel formation than the pressure-untreated native protein. This observation can be explained by assuming that the pressure unfolded-refolded protein is in a misfolded state, which is more stable than the native one.
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