Abstract
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 imaging (SPRi). Conclusion: Our study provides a feasible scheme for confirming the interaction of chemical compounds and cellular binding peptides.Keywords: Strychnine, phage display, biopanning, binding peptide, proliferation assays, diffusion assays, surface plasmon resonance imaging.
Graphical Abstract
Protein & Peptide Letters
Title:Identification and Characterization of Strychnine-Binding Peptides Using Phage-Display Screening
Volume: 24 Issue: 7
Author(s): Fang Zhang, Min Wang*, Zheng Qiu*, Xiao-Meng Wang, Chun-lei Xu and Xia Zhang
Affiliation:
- School of Life Science & Biotechnology, China Pharmaceutical University, Nanjing,China
- School of Life Science & Biotechnology, China Pharmaceutical University, Nanjing,China
Keywords: Strychnine, phage display, biopanning, binding peptide, proliferation assays, diffusion assays, surface plasmon resonance imaging.
Abstract: 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 imaging (SPRi). Conclusion: Our study provides a feasible scheme for confirming the interaction of chemical compounds and cellular binding peptides.Export Options
About this article
Cite this article as:
Zhang Fang , Wang Min *, Qiu Zheng *, Wang Xiao-Meng , Xu Chun-lei and Zhang Xia , Identification and Characterization of Strychnine-Binding Peptides Using Phage-Display Screening, Protein & Peptide Letters 2017; 24 (7) . https://dx.doi.org/10.2174/0929866524666170404164408
DOI https://dx.doi.org/10.2174/0929866524666170404164408 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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