Stable Misfolded States of Human Serum Albumin Revealed by High-pressure Infrared Spectroscopic Studies

Overview

Journal Eur Biophys J

Specialty Biophysics

Date 2008 Feb 16

PMID 18274741

Citations 3

Authors

L Smeller

F Meersman

K Heremans

Affiliations

Soon will be listed here.

Abstract

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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