The Phylomer® library consists of protein fragments, which have been sourced from an evolutionary diverse range of bacterial genomes. These bacteria have been collected from diverse and often harsh environments, in which their genomes have been subject to intense natural selection to evolve the most stable protein structures, that facilitate their survival. Consequently, the Phylomer® libraries are highly enriched for stable sub-domains (15-50 amino acids long) of natural proteins, which we refer to as Phylomer® peptides. These Phylomer® peptides provide a rich source of high affinity peptide disruptors of protein interactions and binders of protein targets. Importantly, the Phylomer® libraries, consist of an enormously diverse collection of stable peptide structures representing millions of potential drug candidates.

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Phylogica has refined the process of drug discovery using the Phylomer® libraries and integrating this technology with high throughput screening platforms such as Phage Display and Yeast-two-hybrid. These screening techniques facilitate rapid sampling of the Phylomer® libraries for the structures and shapes that most efficiently bind a protein or disrupt specific protein interaction. This allows Phylogica to target and disrupt protein interactions that are important mediators of disease.

Phylogica has developed a panel of Phylomer® libraries, each containing a unique collection of millions of natural, stable protein segments called Phylomer® peptides, which can be screened for potential drug candidates.

There are a number of variants of the Phylomer® libraries which are tailor made to allow screening depending upon the nature of the target - be it extracellular or intracellular.