The power of CLIPS™

Highly constrained peptides with enhanced affinity, selectivity and proteolytic stability

Pepscan has developed a uniquely versatile and broadly applicable technology for constraining the 3D conformation of peptides, called CLIPSTM (Chemical Linkage of Peptides onto Scaffolds). Unlike other constraining methods, CLIPSTM chemistry can create redox-stable mono-, bi- or tri-cyclic formats1) and is compatible with the presence of side-chain-unprotected amino acids. CLIPSTM peptides have shown their benefits in many areas.

Validation of 1-CLIPS Platform - Finding the right CLIPS for each target


One of the absolute strengths of this technology is the wide structural diversity of different CLIPSTM scaffolds that can be used, be it hydrophobic or hydrophilic in nature, or with very different sizes and bite angles. We currently have a selection of well over 50 different scaffolds, a number that grows every year. The strength of CLIPSTM is that every scaffold has a unique binding mode, which means that the binding of peptides attached to it changes when the nature of the scaffold has changed.



Small Molecule Drugs

Molecular Weight (kDa)

> 10

~ 2.5

~ 0.5

Target Specificity

Benign Metabolic Pathway

Off-target toxicity


Tissue penetration

Cost of goods

Speed/cost of discovery

1) The “bicyclic peptide domain is further developed by Bicycle Therapeutics since a technological cooperation started in 2009. For this reason Pepscan has no freedom to use bicyclic peptides in Phage Display

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