Pepticom’s technology is centered around the concept that unique peptide drug candidates can be designed by artificial intelligence based solely on the 3D structure of the target protein. This make Pepticom the forerunner of peptide discovery, as our platform is independent of previous screening attempts, unlike the majority of rational drug design platforms. The increase in publicly available structural data, coupled with massive computing power drive a synergy that puts artificial intelligence discovery platforms in the frontline of future drug discovery.
The software analyzes the target surface surrounding the desired binding area. It then performs a complex design process, until eventually converging on to a diversified peptide library of optimal binding affinity.
Linear peptides are defined by having no organized secondary backbone structure, thus binding as a “loose or random coil”. These peptides are noted by being very flexible, able to target varied areas of surface geometry. Small linear peptides are ideal for further development into small molecules/ peptidomimetics.
Peptide Helices have organized secondary backbone structure thus are more rigid than “loose coils”. They can fit into large protein pockets, grooves and even flat surfaces. Due to the helical structure, the backbone atoms are more “protected” from proteolytic enzymes which often leads to better serum stability. Additionally, rigid structure potentially enables better binding affinities.
Cyclic peptides are peptide molecules containing a bond that generates a ring. Cyclic Peptide, like helical peptides, possess conformational restrictions on the backbone making them less susceptible to proteolytic cleavage thus characterized as having better serum stability. Additionally, the conformational restrictions potentially provides greater affinity. Cyclic peptides are often smaller than Helices peptides, thus having a superior ability to penetrate the cell membrane.
D-amino-acids are the mirror images of the natural occurring L-amino- acids and are rarely present in natural substances. Since they differ in 3D orientation than L-amino acids, they are less susceptible to proteolytic cleavage and are thus tend to have better serum stability. This peptide design module can be integrated into LINEPEP, CYCPEP and HELPEP.
The module is underway with initial proof of concept already validated in the lab.
Pepticom is currently the only platform for the discovery of N to C cyclic peptides.
Validated active peptides can be implemented in a 3D pharmacophore model, used for the screening small molecules that are structurally unrelated to the peptide, but can fill points in space that are crucial for binding.
Pepticom’s technology enables peptides modification with non- natural amino acids. Validated laboratory peptides can undergo structure optimization aimed at improving peptides’ binding affinity while granting certain protection from enzymatic catalysis.
Pepticom’s technology enables the discovery of peptide scaffolds capable of stabilizing mutated protein. This capability is not possible in traditional screening techniques. This capability was demonstrated in a scientific paper published recently in collaboration with Hadassah Medical Center and Oxford University (https://hmg.oxfordjournals.org/ content/early/2015/08/04/hmg.ddv280.full)