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Light-activated affinity micropatterning of proteins

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2 Author(s)
Yang, Z.P. ; Dept. of Biomed. Eng., Duke Univ., Durham, NC, USA ; Chikoti, A.

Protein micropatterning has attracted considerable interest because of its prospective application in the fabrication of biosensors and tissue engineering substrates. Motivated by these potential applications, we have developed a method to micropattern proteins onto self-assembled monolayers (SAMs) on gold, which we term light-activated affinity micropatterning of proteins (LAMP). LAMP is a multi-step patterning process: first, a gold substrate is modified with a mixture of 11-mercaptoundecanol and 16-mercaptohexadecanoic acid to provide a non-fouling, reactive SAM template on gold. Next, the carboxylic acid terminal groups in the binary SAM are coupled to methylnitropiperonyloxy-carbonyl biotin, (“caged” biotin) through a diamine linker, resulting in a mixed MeNPOC-biotinyl/OH-terminated monolayer. Activation of the caged biotin by spatially-defined UV illumination at 350-360 nm reconstitutes biotin in the illuminated region, allowing streptavidin or anti-biotin antibody to be localized in the illuminated regions. We have investigated each fabrication step in LAMP by a variety of surface analytical techniques, including contact angle goniometry, ellipsometry, surface plasmon resonance, and X-ray photoelectron spectroscopy to optimize ligand density and pattern contrast. LAMP can be further extended to spatially-resolved micropatterning of multiple biomolecules by repeated cycles of spatially-defined activation, streptavidin incubation, followed by binding of the biotinylated moiety of interest

Published in:

[Engineering in Medicine and Biology, 1999. 21st Annual Conference and the 1999 Annual Fall Meetring of the Biomedical Engineering Society] BMES/EMBS Conference, 1999. Proceedings of the First Joint  (Volume:2 )

Date of Conference:

Oct 1999