| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 746615 | Sensors and Actuators B: Chemical | 2009 | 5 Pages |
Surface plasmon resonance and phage display technique were combined to acquire abundant specific capture molecules and realize label-free and high-sensitive detection for the protein chip. The 12-amino acid peptide displayed on phage M13 coated protein pIII (ET101-4-11) was selected as the probe, it was immobilized on 11-mercapto-undecanoic acid (11-MUA) sensor chip to fabricate the phage-displayed protein chip, and the interaction between the peptide and the specific protein (ET101) was detected on the BIAcore3000. Experimental results show that when ET101 diluted in series concentrations flow through the sensor chip, the relationship between the response and the sample concentration fits the sigmoid-curve very well, and the ET101 concentration of 4.0 μM corresponds to the response of 365RU ± 8RU. The kinetic parameters are also calculated, including the association rate 4.75 M−1s−1 and the dissociation rate 2.76 × 10−3s−1. The research suggests that the phage-displayed protein chip can act as a useful tool in proteomics research.
