Background: In drug development, phage display is a high-throughput method for identifying
the specific cellular targets of drugs. However, insoluble small chemicals remain intractable
to this technique because of the difficulty of presenting molecules to phages without occupying or
destroying the limited functional groups.
Objectives: In the present study, we selected Strychnine (Stry) as a model compounda and sought to
develope an alternative in vitro biopanning strategy against insoluble suspension.
Method: A phage library displaying random sequences of fifteen peptides was employed to screen
for interactions between Stry and its cellular selective binding peptides, which are of great value to
have a complete understanding of the mechanism of Stry for its antitumor activity.
Results: After four rounds of biopanning, a selection of 100 binding clones was randomly picked
and subjected to modified proliferation and diffusion assays to evaluate the binding affinity of the
clones. Finally, eleven clones were identified as positive binders. The corresponding peptides
were synthesized and detected for their binding activities using surface plasmon resonance
Conclusion: Our study provides a feasible scheme for confirming the interaction of chemical
compounds and cellular binding peptides.