title: Chemical-vapor-deposition-based polymer substrates for spatially resolved analysis of protein binding by imaging ellipsometry.
abstract: Biomolecular interactions between proteins and synthetic surfaces impact diverse biomedical fields. Simple, quantitative, label-free technologies for the analysis of protein adsorption and binding of biomolecules are thus needed. Here, we report the use of a novel type of substrate, poly-p-xylylene coatings prepared by chemical vapor deposition (CVD) polymerization, for surface plasmon resonance enhanced ellipsometry (SPREE) studies and assess the reactive coatings as spatially resolved biomolecular sensing arrays. Prior to use in binding studies, reactive coatings were fully characterized by Fourier transform infrared spectroscopy, electrochemical impedance spectroscopy, and ellipsometry. As a result, the chemical structure, thickness, and homogeneous coverage of the substrate surface were confirmed for a series of CVD-coated samples. Subsequent SPREE imaging and fluorescence microscopy indicated that the synthetic substrates supported detectable binding of a cascade of biomolecules. Moreover, analysis revealed a useful thickness range for CVD films in the assessment of protein and/or antigen-antibody binding via SPREE imaging. With a variety of functionalized end groups available for biomolecule immobilization and ease of patterning, CVD thin films are useful substrates for spatially resolved, quantitative binding arrays.
authors.affiliation: Department of Biomedical Engineering, University of Michigan, Ann Arbor, Michigan 48109, USA.
authors.forename: Aftin M
authors.initials: AM
authors.lastname: Ross
authors.forename: Di
authors.initials: D
authors.lastname: Zhang
authors.forename: Xiaopei
authors.initials: X
authors.lastname: Deng
authors.forename: Seiwon Laura
authors.initials: SL
authors.lastname: Chang
authors.forename: Joerg
authors.initials: J
authors.lastname: Lahann
mesh_terms: D002623:Chemistry Techniques, Analytical / Q000295:instrumentation / Q000379:methods*; D055664:Electrochemical Techniques / Q000379:methods; D005340:Fibrinogen / Q000032:analysis* / Q000378:metabolism; D018625:Microscopy, Atomic Force; D015394:Molecular Structure; D011108:Polymers / Q000737:chemistry*; D011485:Protein Binding; D014835:Volatilization
chemical_list: D011108:Polymers; D005340:Fibrinogen