Protein adsorption at air-water interfaces: A combination of details

Using a variety of spectroscopic techniques, a number of molecular functionalities have been studied in relation to the adsorption process of proteins to air–water interfaces. While ellipsometry and drop tensiometry are used to derive information on adsorbed amount and exerted surface pressure, exte...

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Bibliographic Details
Published in:Biopolymers 2004-05, Vol.74 (1-2), p.131-135
Main Authors: de Jongh, Harmen H. J., Kosters, Hans A., Kudryashova, Elena, Meinders, Marcel B. J., Trofimova, Daria, Wierenga, Peter A.
Format: Article
Language:English
Subjects:
Adsorption
Air
air-water interfaces
Animals
Biophysical Phenomena
Biophysics
Carboxylic Acids - chemistry
Cattle
Chickens
Circular Dichroism
drop tensiometry
ellipsometry
external reflection
fluorescence
Hydrogen-Ion Concentration
infrared
Kinetics
Pressure
Proteins - chemistry
Spectrometry, Fluorescence - methods
Spectrophotometry, Infrared - methods
Static Electricity
Surface Properties
Time Factors
Water - chemistry
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Summary:Using a variety of spectroscopic techniques, a number of molecular functionalities have been studied in relation to the adsorption process of proteins to air–water interfaces. While ellipsometry and drop tensiometry are used to derive information on adsorbed amount and exerted surface pressure, external reflection circular dichroism, infrared, and fluorescence spectroscopy provide, next to insight in layer thickness and surface layer concentration, molecular details like structural (un)folding, local mobility, and degree of protonation of carboxylates. It is shown that the exposed hydrophobicity of the protein or chemical reactivity of solvent‐exposed groups may accelerate adsorption, while increased electrostatic repulsion slows down the process. Also aggregate formation enhances the fast development of a surface pressure. A more bulky appearance of proteins lowers the collision intensity in the surface layer, and thereby the surface pressure, while it is shown to be difficult to affect protein interactions within the surface layer on basis of electrostatic interactions. This work illustrates that the adsorption properties of a protein are a combination of molecular details, rather than determined by a single one. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004
ISSN:0006-3525
1097-0282
DOI:10.1002/bip.20036