Peptide ligand-protein interactions play a crucial role in signal transduction and cellular functions. To identify high-affinity and high-specificity peptide ligands among thousands of competitors, a rapid and robust screening method is required. Fortunately, phage-displayed peptide libraries have proven to be an effective tool for exploring peptide ligands.
The development of peptide ligands has broad application prospects, including:
Creative Biolabs provides a high-throughput and rapid method for sequencing peptide ligands isolated from the screening, which capitalizes on next-generation DNA sequencing and bioinformatics analysis of the selected phage clones. In combination with our high-quality premade peptide libraries, we can provide up to 300 unique bioactive peptides for a variety of targets in a short time.
Creative Biolabs offers the high-throughput Magic™ platform for bioactive peptide discovery. This powerful platform rapidly characterizes all clones in the screened library to identify one or more peptide families that specifically bind to the target protein. The main steps are as follows:
Create a phage display library containing a diverse range of peptide sequences. These sequences are randomly displayed on the phage surface, offering numerous potential binding peptides.
Incubate the library with the target protein (such as receptors, enzymes, antibodies, etc.) to allow specific binding. Wash away unbound phages, retaining only those that bind to the target protein.
Recover phages that bind to the target protein and amplify them to increase the number of specific binding peptides. Repeat this screening and amplification process (known as panning) for multiple rounds (typically three to five) to improve specificity and enrichment.
Use next-generation DNA sequencing (NGS) to sequence the selected phages and obtain the peptide sequences they display. Perform bioinformatics analysis to identify peptides with high affinity and specificity for the target protein.
Validate the binding ability of the selected candidate peptides in vitro. Further improve peptide affinity and stability through mutagenesis and optimization strategies, producing highly active peptide ligands.
Fig.1 Phage display for peptides and antibodies discovery.1
Fig. 2 The peptide sequences of the selected cyclic heptapeptide libraries were determined through sequencing.
Our laboratory developed highly specific cyclic heptapeptides that can bind to target proteins and reconstitute them. Through sequencing, we identified the peptide sequences of the selected cyclic heptapeptide library and discovered several potential candidate peptides.
A: There are several types of phage libraries available, including M13 phage libraries, T7 phage libraries, cDNA libraries, and constrained peptide libraries. Each type is designed to display a diverse range of peptides or proteins that can be screened against your target of interest.
A: Specificity is ensured through multiple rounds of panning (binding, washing, and elution) with increasing stringency in the washing steps. Additionally, negative selection steps can be included to remove peptides that bind to non-target molecules.
A: Yes, once high-affinity peptides are identified through phage display, they can be synthesized chemically for further use in research, therapeutic development, or diagnostic applications. These peptides can also be modified to enhance their stability, affinity, or specificity.
A: Yes, once high-affinity peptides are identified, they can be chemically synthesized and modified to enhance their stability, affinity, or specificity. Modifications may include cyclization, incorporation of non-natural amino acids, or conjugation to other molecules.
If you are interested or have a current requirement for high-affinity peptide ligands, please do not hesitate to
. Creative Biolabs is here to support your projects with cutting-edge technology and unparalleled expertise.Use the resources in our library to help you understand your options and make critical decisions for your study.
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