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Bursting the bubble; how surfactants destabilize protein foams, revealed by atomic force microscopy
Author(s) -
Patrick Gunning A.,
Mackie Alan R.,
Wilde Peter J.,
Morris Victor J.
Publication year - 1999
Publication title -
surface and interface analysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.52
H-Index - 90
eISSN - 1096-9918
pISSN - 0142-2421
DOI - 10.1002/(sici)1096-9918(199905/06)27:5/6<433::aid-sia486>3.0.co;2-r
Subject(s) - pulmonary surfactant , nucleation , bubble , adsorption , atomic force microscopy , chemistry , chemical physics , displacement (psychology) , homogeneous , amphiphile , chemical engineering , nanotechnology , crystallography , biophysics , materials science , thermodynamics , mechanics , physics , organic chemistry , biochemistry , biology , engineering , copolymer , polymer , psychology , psychotherapist
The bubbles in a pure protein foam are stabilized by elasticnetworks of protein molecules that adsorb to the air/waterinterface through hydrophobic interaction. In real systems, however,there are often other amphiphiles present that have an antagonisticeffect on the stability of the foam. This paper describes the firstdirect observation of specific heterogeneous structures that occurduring the competitive adsorption between proteins and surfactants.This is in contrast to the previous assumption of a homogeneousdistribution of the two competing species at the interface. By usingatomic force microscopy to visualize the breakdown of proteinnetworks, we have identified the specific mechanism for surfactantdisplacement of proteins from an air/water interface. Thismechanism, which we have termed an orogenic model of proteindisplacement, involves nucleation and growth of surfactant domainsthat compress and then fracture the protein network, eventuallyinducing its displacement from the interface. Copyright © 1999John Wiley & Sons, Ltd.