Removing the trial and error testing and complexity of Protein-Protein Interactions
Our evolutionary algorithms find the best PPI binding events by simulating topological fit, electrostatic forces, hydrogen bonding, and hydrophobic effect.
Head-to-Tail Staple
Unique capability of structure-based de novo design. The evolutionary algorithm generates a new fragment that is compatible with the existing part. The original helix and the staple are therefore seamlessly complementary, much more so than the conventional "stapled peptides" methodology usually allows.
Helix Hybrid Design
Example of hybrid design. Existing helix stabilized by the addition of a designer head-to-tail link.
Peptide Modification
Our proprietary molecular design technology relies on the Monte Carlo scheme, which automatically generates compatible, synthetically available peptides within the "evolutionary constraints" provided by the structure of the receptor, the composition of the library of amino acids, and the self-compatibility of the generated molecular assembly.
Phage Display
Our design protocol is free from the inherent limitation of the currently predominant phage display approach. De novo design is capable of freely combining the natural amino acids with non-proteinogenic ones, and incorporating post-translational modifications. We are particularly interested in conformationally and proteolytically stable macrocyclic peptides.
