27 December 2007 Simple micropatterning of proteins using polyelectrolyte multilayers and microcontact printing
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Abstract
The selective immobilization of various biomolecules in well-defined area is important technique for the development of biosensors and biochips. Especially, the fabrication of protein micropatterns preserving their functional activity on the desired surface is critical issue for the development of medical diagnostic devices and basic protein studies. In this study, we have introduced a simple but reliable method of protein patterning on functionalized polyelectrolyte thin films (PEL) through consecutive layer-by-layer adsorption of polyelectrolytes via self-assembly technique and microcontact printing (μCP). For the selection of appropriate surface, several representative surfaces modified with various functional materials including aldehyde, epoxide, poly-L-lysine, amine, and self-assembled polyelectrolyte multilayers (PEL) were investigated. The PEL surface providing electrostatic interaction force showed most high functionality in point of homogeneous patterning of proteins with high density and preservation of inherent 3-dimensional structure of proteins. Immunoassay as a model system of protein-protein interaction showed good linearity, indicating the feasibility of a quantitative measurement of the concentration of target proteins in sample. Our proposed approach based on PEL constructed by self-assembly technique in aqueous solution is green chemistry and cost-effective method to generate stable 3-D thin film on surface. The demand for strict control over the positioning and the stable immobilization of several kinds of biomolecules in fabricated structures can result in many applications.
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Ji-Hye Lee, Ji-Hye Lee, Chang-Hyung Choi, Chang-Hyung Choi, Chang-Soo Lee, Chang-Soo Lee, } "Simple micropatterning of proteins using polyelectrolyte multilayers and microcontact printing", Proc. SPIE 6799, BioMEMS and Nanotechnology III, 67991F (27 December 2007); doi: 10.1117/12.768573; https://doi.org/10.1117/12.768573
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