Microcontact Printed Antibodies on Gold Surfaces: Function, Uniformity, and Silicone Contamination

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• 作者：Jennifer O. Foley ; Elain Fu ; Lara J. Gamble ; Paul Yager
• 刊名：Langmuir
• 出版年：2008
• 出版时间：April 1, 2008
• 年：2008
• 卷：24
• 期：7
• 页码：3628 - 3635
• 全文大小：248K
• 年卷期：v.24,no.7(April 1, 2008)
• ISSN：1520-5827

文摘

The function of microcontact printed protein was investigated using surface plasmon resonance (SPR) imaging,X-ray photoelectron spectroscopy spectroscopy (XPS), and XPS imaging. We chose to analyze a model protein system,the binding of an antibody from solution to a microcontact printed protein antigen immobilized to a gold surface. SPRimaging experiments indicated that the microcontact printed protein antigen was less homogeneous, had increasednonspecific binding, and bound less antibody than substrates to which the protein antigen had been physically adsorbed.SPR images of substrates contacted with a poly(dimethylsiloxane) stamp inked with buffer alone (i.e., no protein)revealed that significant amounts of silicone oligomer were transferred to the surface. The transfer of the siliconeoligomer was not homogeneous, and the oligomer nonspecifically bound protein (BSA and IgG) from solution. XPSspectroscopy and imaging were used to quantify the amount of silicon (due to the presence of silicone oligomer), aswell as the amounts of other elements, transferred to the surface. The results suggest that the silicone oligomerintroduced by the printing process reduces the overall binding capacity of the microcontact-printed protein comparedto physically adsorbed protein.