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Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes
Published on: October 3, 2019
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Selection of Peptide-Bismuth Bicycles Using Phage Display
Ruo-Nan He1,2,3, Meng-Jie Zhang2,3, Bin Dai1
1School of Sensing Science and Engineering, School of Electronic Information and Electrical Engineering, Shanghai Jiao Tong University, 800 Dongchuan Road, Shanghai 200240, China.
ACS Chemical Biology
|April 15, 2024
Summary
Bismuth (Bi3+) ions enable cysteine conjugation for phage display peptide cyclization. This method enhances peptide affinity, accelerating the development of novel peptide-bismuth therapeutics.
Area of Science:
- Biotechnology and Pharmaceutical Sciences
- Peptide Chemistry and Engineering
Background:
- Cysteine conjugation is a standard technique for constraining phage-displayed peptides, enabling the selection of cyclic peptides.
- Phage display technology is a powerful tool for identifying high-affinity ligands against specific biological targets.
Purpose of the Study:
- To investigate the use of nontoxic Bismuth (Bi3+) ions as a cysteine conjugation reagent for phage-displayed peptide libraries.
- To evaluate the feasibility of Bi3+-mediated cyclization for selecting high-affinity bicyclic peptides against a model target.
Main Methods:
- Construction and Bi3+-mediated cyclization of a randomized 3-cysteine peptide library displayed on phage.
- Selection of cyclized peptides against the maltose-binding protein target using phage display.
- Next-generation sequencing for identifying consensus sequences and affinity validation of synthesized peptides.
Main Results:
- Bi3+ successfully cross-linked peptide libraries without affecting phage infectivity.
- Enrichment of specific consensus sequences was observed after selection against the target protein.
- Bi3+ cyclized peptides demonstrated a hundred-fold improvement in binding affinity compared to their linear counterparts.
Conclusions:
- Bismuth (Bi3+) ions are effective reagents for developing constrained bicyclic peptides via phage display.
- This approach accelerates the discovery of potent peptide-bismuth structures for potential therapeutic and diagnostic applications.
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