Peptides are important molecules in protein drug screening. Using the software that we developed, high-throughput antibody-peptide binding can be visualized for drug screening, including dynamic imaging of antibody-peptide binding for studying specific interactions, visualizing the dynamic profile of antibody-peptide binding in each tunnel to analyze dynamic mechanical processes, and producing three-dimensional histograms of whole tunnels in the SPRi peptide microarray chip for high-throughput drug screening. Figure 5 shows the visualization of antibody-peptide binding, in which the entire antibody-peptide binding process was monitored continuously about 140 min. Figure 5(a) shows 10 images of the mixture of three antibodies (anti-283-2, anti-204-2, anti-200-2) binding to the peptide probe array at 10 different time points (0, 1, 5, 20, 30, 40, 60, 120, 130, and 140 min). The dynamic monitoring signals from the five different probes during antibody-peptide binding correspond to anti-283-2 binding to peptide 283-2, anti-204-2 binding to peptide 204-2, anti-200-2 binding to peptide 200-2, and no molecular binding to the buffer and BSA probes [Fig. 5(b)]. These results indicate that antibody-peptide binding can be detected within 1 min [Fig. 5(a), II]. The signals rose continuously for 120 min and reached a plateau phase at the end [Fig. 5(b)]. The change in the reflected light intensity due to antibody-peptide binding reached an exponential stage within 30 min [Fig. 5(b)]. Figure 5(b) indicates that anti-204-2 binding to peptide 204-2 was the most rapid, and anti-283-2 binding to peptide 283-2 was the strongest.