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Bicyclic Peptide Discovery Based on Two Disulfide Bridges

With years of research and development experience in the field of phage display, Creative Biolabs has owned a group of scientists who are professional in applying advanced phage display technologies to a broad range of project objectives. Through our advanced phage display platform, scientists of Creative Biolabs has employed effective strategy for the phage selection of bicyclic peptides based on two disulfide bridges. Using this strategy, we can screen topologically highly diverse bicyclic peptide structures by phage-displayed combinatorial peptide libraries. We are pleased to use our extensive experience and advanced platform to provide this high-quality service of screening bicyclic peptides for our global customs.

Bicyclic Peptides Properties

Bicyclic peptides are a class of molecules defined by a structure of two connected peptide rings. Cyclization and the close proximity of the two macrocyclic rings limit the conformational flexibility of the peptide backbone and enable binding with high affinity and selectivity to protein targets. They can bind to protein targets with high affinity and selectivity, making them attractive for biotechnological and medicinal applications. The good binding properties are due to the limited conformational flexibility of the two connected peptide rings. Bicyclic peptide can rapidly penetrate a tumor and deliver the payloads selectively, which will minimize the exposure to normal tissue and associated toxicities. Hence, they are a group of new and good therapeutic modality, which usually applied with an antibody, allowing rapid extravasation and tumor penetration.

Bicyclic Peptide Discovery Based on Two Disulfide BridgesFig.1 Phage selection of bicyclic peptides based on two disulfide bridges (Chen & Heinis 2015).

Bicyclic Peptide Discovery Based on Two Disulfide Bridges

Creative Biolabs has developed a technically simple and robust strategy to screen bicyclic peptides based on two disulfide bridges by phage-displayed combinatorial peptide libraries. Our scientists are proficient in constructing large combinatorial peptide libraries (up to 1011) of different formats (e.g., CX6CX6C or XCX4CX4CX, C=cysteine, X=any random amino acid). The cysteines in the peptides oxidize to form disulfide bridges during the production in the periplasmic space of bacteria or in the culture media. We perform the biopanning on our advanced phage display platform. For the phage affinity selection, the phages are washed and eluted with a buffer having a low pH. Our strategies can be adapted to generate bicyclic peptide libraries of any desired format and to isolate binders to any protein target. Combined with Magic™ Sequencing, bicyclic peptides in the enriched sublibrary can be identified efficiently and effectively.

Key Advantages


Equipped with world-leading technology platforms and professional scientific staff in phage display platform, Creative Biolabs is pleased to share our cutting-edge technology and extensive expertise in phage selection of bicyclic peptides based on two disulfide bridges. We can offer high-quality customized services by adjusting protocols to meet our clients’ specific requirements.

For more detailed information, please feel free to contact us or directly send us an inquiry.

Reference

  1. Chen, S.; Heinis, C. Phage selection of bicyclic peptides based on two disulfide bridges. Methods Mol Biol. 2015, 1248:119-37.

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