Stable misfolded states of human serum albumin revealed by high-pressure infrared spectroscopic studies

L. Smeller, F. Meersman, K. Heremans

Research output: Contribution to journalArticle

11 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1127-1132
Number of pages6
JournalEuropean Biophysics Journal
Volume37
Issue number7
DOIs
Publication statusPublished - Sep 2008

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Serum Albumin
Pressure
Protein Refolding
Protein Unfolding
Deuterium
Fourier Analysis
Decompression
Hydrogen
Gels
Temperature
Proteins

Keywords

  • Aggregation
  • Conformational disease
  • High pressure
  • Human serum albumin
  • Infrared
  • Misfolding
  • Spectroscopy

ASJC Scopus subject areas

  • Biophysics

Cite this

Stable misfolded states of human serum albumin revealed by high-pressure infrared spectroscopic studies. / Smeller, L.; Meersman, F.; Heremans, K.

In: European Biophysics Journal, Vol. 37, No. 7, 09.2008, p. 1127-1132.

Research output: Contribution to journalArticle

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