TY - JOUR
T1 - Protein adsorption on poly(N -isopropylacrylamide) brushes
T2 - Dependence on grafting density and chain collapse
AU - Xue, Changying
AU - Yonet-Tanyeri, Nihan
AU - Brouette, Nicolas
AU - Sferrazza, Michele
AU - Braun, Paul V.
AU - Leckband, Deborah E.
PY - 2011/7/19
Y1 - 2011/7/19
N2 - The protein resistance of poly(N-isopropylacrylamide) brushes grafted from silicon wafers was investigated as a function of the chain molecular weight, grafting density, and temperature. Above the lower critical solution temperature (LCST) of 32 °C, the collapse of the water-swollen chains, determined by ellipsometry, depends on the grafting density and molecular weight. Ellipsometry, radio assay, and fluorescence imaging demonstrated that, below the lower critical solution temperature, the brushes repel protein as effectively as oligoethylene oxide-terminated monolayers. Above 32 °C, very low levels of protein adsorb on densely grafted brushes, and the amounts of adsorbed protein increase with decreasing brush-grafting-densities. Brushes that do not exhibit a collapse transition also bind protein, even though the chains remain extended above the LCST. These findings suggest possible mechanisms underlying protein interactions with end-grafted poly(N-isopropyl acrylamide) brushes.
AB - The protein resistance of poly(N-isopropylacrylamide) brushes grafted from silicon wafers was investigated as a function of the chain molecular weight, grafting density, and temperature. Above the lower critical solution temperature (LCST) of 32 °C, the collapse of the water-swollen chains, determined by ellipsometry, depends on the grafting density and molecular weight. Ellipsometry, radio assay, and fluorescence imaging demonstrated that, below the lower critical solution temperature, the brushes repel protein as effectively as oligoethylene oxide-terminated monolayers. Above 32 °C, very low levels of protein adsorb on densely grafted brushes, and the amounts of adsorbed protein increase with decreasing brush-grafting-densities. Brushes that do not exhibit a collapse transition also bind protein, even though the chains remain extended above the LCST. These findings suggest possible mechanisms underlying protein interactions with end-grafted poly(N-isopropyl acrylamide) brushes.
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U2 - 10.1021/la2001909
DO - 10.1021/la2001909
M3 - Article
C2 - 21662243
AN - SCOPUS:79960286171
SN - 0743-7463
VL - 27
SP - 8810
EP - 8818
JO - Langmuir
JF - Langmuir
IS - 14
ER -