Nanosystems for biosensing: multianalyte immunoassay on a protein chip.
This chapter describes the construction of addressable two-dimensional (2D) microarrays via the random fluidic self-assembly of metallic particles and the use of these arrays as platforms for constructing protein chips for bioassays. These arrays will be useful as platforms for constructing protein chips for bioassays in a broad range of applications. The basic units in the assembly are microfabricated particles, which carry a straightforward visible code, and the corresponding array template patterned on a glass substrate. On one face, the particles consist of a hydrophobic and magnetic Ni-polytetrafluoroethylene (Ni-PTFE) composite layer; the other face has a gold layer that was modified for biomolecular attachment. We use photoresist patterning to create an array template with spatially discrete microwells into which an Ni-PTFE hydrophobic composite layer and a hydrophobic photoadhesive coating are electrodeposited. After biomaterial attachment and binding processes in bulk, the particles are randomly self-assembled onto the lubricated bonding sites on the chip substrate. This self-assembly process is driven by a combination of magnetic, hydrophobic, and capillary interactions. The encoding symbol carried by each particle is used to identify the target attached to the particle surface. This model system demonstrates the utility of the protein chip array for conducting simultaneous multianalyte immunoassays of human immunoglobulins (IgA, IgG, and IgM).
Tamiya
Eiichi
E
School of Materials Science, Japan Advanced Institute of Science and Technology, Ishikawa, Japan.
Zhi
Zheng-Liang
ZL
Morita
Yasutaka
Y
Hasan
Quamrul
Q
D000818:Animals; D015374:Biosensing Techniques / Q000379:methods*; D006801:Humans; D007118:Immunoassay / Q000379:methods; D007136:Immunoglobulins / Q000032:analysis; D008163:Luminescent Measurements / Q000379:methods; D036103:Nanotechnology / Q000379:methods*; D040081:Protein Array Analysis / Q000379:methods*
D007136:Immunoglobulins