CLIPS scaffolds used in phage display to boost drug discovery
Phage display is a technology that allows de novo discovery of peptidic binders against any protein target of interest by exploring DNA-encoded peptide libraries, exceeding billions of different members. Our team of experts developed a unique phage display platform for the discovery of high-quality lead candidates with affinity for clients’ targets.
Unique CLIPS scaffold portfolio
By incorporating Pepscan’s unique CLIPS scaffold portfolio, we optimized our phage display platform for the identification of CLIPS constrained peptides, a class of highly-constrained peptides displaying enhanced affinity, selectivity and proteolytic stability, and well-suited for diagnostic and therapeutic applications. This methodology gives researchers the opportunity to target more diverse epitopes on target proteins and to improve the chance of identifying peptides with higher affinities and specificities, due to a more thorough exploration of the existing conformational space.
Our CLIPS portfolio contains over 25 different scaffold molecules, which in combination with ingeniously composed phage-display peptide libraries based on trinucleotide technology and diversities exceeding 4E+10 variants yield libraries of monocyclic CLIPS-peptides. This combination serves two purposes:
- It helps create additional contacts between the CLIPS scaffolds and hydrophobic, aromatic or cationic residues on the target’s surface, resulting in unique lead candidates;
- Combining monocyclic libraries with different types of CLIPs aids the exploration of different conformational assembles in the peptide structural space, leading to the identification of unique lead candidates.
Our Chief Scientific Officer Peter Timmerman invented the CLIPS constraining technology and has world-leading expertise in the synthesis of CLIPS-constrained peptides in various formats and scales, making Pepscan the ideal partner to support the optimization and (GMP) production of your selected candidates.