TY - JOUR
T1 - Comparison of resistance to protein adsorption and stability of thin films derived from α-hepta-(ethylene glycol) methyl ω-undecenyl ether on HSi(111) and HSi(100) surfaces
AU - Yam, Chi Ming
AU - Gu, Jianhua
AU - Li, Sha
AU - Cai, Chengzhi
N1 - Funding Information:
This work was supported by the Welch Foundation, National Science Foundation (CTS-0210840), and University of Houston (GEAR and TcSAM Special Funding).
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2005/5/15
Y1 - 2005/5/15
N2 - Oligo(ethylene glycol)-terminated thin films were prepared by photo-induced hydrosilylation of α-hepta-(ethylene glycol) methyl ω-undecenyl ether (EG7) on hydrogen-terminated silicon (111) and (100) surfaces. Their resistance to protein adsorption, and stabilities (from hours to days) under a wide variety of conditions, such as air, water, biological buffer, acid, and base, were investigated using contact-angle goniometry and ellipsometry techniques. Results indicated higher stability of the films chemisorbed on Si(111) than on Si(100). Furthermore, micron-sized patterns were fabricated on the films via AFM anodization lithography. Using atomic force microscopy (AFM) and fluorescence microscopy, we demonstrated that various proteins including fibrinogen, avidin, and bovine serum albumin (BSA) predominately adsorbed onto the patterns, but not the rest of the film surfaces.
AB - Oligo(ethylene glycol)-terminated thin films were prepared by photo-induced hydrosilylation of α-hepta-(ethylene glycol) methyl ω-undecenyl ether (EG7) on hydrogen-terminated silicon (111) and (100) surfaces. Their resistance to protein adsorption, and stabilities (from hours to days) under a wide variety of conditions, such as air, water, biological buffer, acid, and base, were investigated using contact-angle goniometry and ellipsometry techniques. Results indicated higher stability of the films chemisorbed on Si(111) than on Si(100). Furthermore, micron-sized patterns were fabricated on the films via AFM anodization lithography. Using atomic force microscopy (AFM) and fluorescence microscopy, we demonstrated that various proteins including fibrinogen, avidin, and bovine serum albumin (BSA) predominately adsorbed onto the patterns, but not the rest of the film surfaces.
KW - AFM anodization lithography
KW - Hydrogen-terminated silicon surfaces
KW - Oligo(ethylene glycol)-terminated thin films
KW - Photo-induced surface hydrosilylation
KW - Protein adsorption
KW - Stability
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U2 - 10.1016/j.jcis.2004.12.007
DO - 10.1016/j.jcis.2004.12.007
M3 - Article
C2 - 15837490
AN - SCOPUS:17444367367
VL - 285
SP - 711
EP - 718
JO - Journal of Colloid And Interface Science
JF - Journal of Colloid And Interface Science
SN - 0021-9797
IS - 2
ER -