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Reduction of albumin adsorption onto silicon surfaces by Tween 20
Author(s) -
Zhang Miqin,
Ferrari Mauro
Publication year - 1997
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19971220)56:6<618::aid-bit4>3.0.co;2-q
Subject(s) - adsorption , pulmonary surfactant , chemistry , protein adsorption , ellipsometry , contact angle , silicon , micelle , albumin , chromatography , chemical engineering , molecule , inorganic chemistry , organic chemistry , materials science , thin film , nanotechnology , biochemistry , aqueous solution , engineering
The ability of Tween 20 to reduce the adsorption of albumin on silicon surfaces of different hydrophobicity was investigated by ellipsometry. As expected, protein adsorption was found to depend on the degree of hydrophobicity of the surfaces and on the concentration of the surfactant. A reduction of 90% in albumin adsorption on hydrophobic methylated surfaces by 0.05% Tween 20 was achieved, whereas a reduction of only 15% on hydrophilic surfaces was observed. Experiments of time‐dependent protein adsorption in both pure protein and protein‐surfactant mixtures were conducted to ascertain the stability of physically adsorbed Tween 20 films on intermediate silicon surfaces. It was found that the adsorbed Tween 20 film was robust and there was no evidence of exchange of the Tween molecules with albumin for up to 240 min exposure. Adsorption minima were confirmed to correlate with minima in contact angle and critical micelle concentration (CMC). © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 56: 618–625, 1997.