Abstract
Protein chip, a powerful high-throughput tool to study protein function, plays a prominent role in the basic research and drug discovery. We have applied a systematic procedure to characterize and evaluate the surface chemistry on the well-known alkyl monolayer modified Si(1 1 1) surface. Protein molecules are immobilized on the surface through chemical bonds, and the specific recognition is observed. The surface protein density has been determined by the combination of Atomic Force Microscopy and immobilization kinetics. The affinity of the surface immobilized IgG molecules is examined by fluorescence detection incorporated with the Langmuir isotherm. In addition, specificity, sensitivity, and homogeneity are also discussed.
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