Driving Force Behind Adsorption-Induced Protein Unfolding: A Time-Resolved X-ray Reflectivity Study on Lysozyme Adsorbed at an Air/Water Interface

Time-resolved X-ray reflectivity measurements for lysozyme (LSZ) adsorbed at an air/water interface were performed to study the mechanism of adsorption-induced protein unfolding. The time dependence of the density profile at the air/water interface revealed that the molecular conformation changed si...

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Bibliographic Details
Published in:Langmuir 2009-01, Vol.25 (1), p.32-35
Main Authors: Yano, Yohko F, Uruga, Tomoya, Tanida, Hajime, Toyokawa, Hidenori, Terada, Yasuko, Takagaki, Masafumi, Yamada, Hironari
Format: Article
Language:English
Subjects:
Adsorption
Air
Chemistry
Colloidal state and disperse state
Exact sciences and technology
General and physical chemistry
Kinetics
Muramidase - chemistry
Protein Denaturation
Surface physical chemistry
Surface Properties
Water
X-Rays
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Summary:Time-resolved X-ray reflectivity measurements for lysozyme (LSZ) adsorbed at an air/water interface were performed to study the mechanism of adsorption-induced protein unfolding. The time dependence of the density profile at the air/water interface revealed that the molecular conformation changed significantly during adsorption. Taking into account previous work using Fourier transform infrared (FTIR) spectroscopy, we propose that the LSZ molecules initially adsorbed on the air/water interface have a flat unfolded structure, forming antiparallel β-sheets as a result of hydrophobic interactions with the gas phase. In contrast, as adsorption continues, a second layer forms in which the molecules have a very loose structure having random coils as a result of hydrophilic interactions with the hydrophilic groups that protrude from the first layer.
ISSN:0743-7463
1520-5827
DOI:10.1021/la803235x