Competitive Advantages of Phylomer® Peptides over Antibodies

Phylogica’s approach to developing peptide-based therapeutics confers many advantages over conventional strategies for biopharmaceutical drug development, particularly antibody-based therapies. These advantages include no antibody royalty stack, manufacturing advantage since they can be synthesized and compatiability with alternative delivery technologies.

Competitive Advantages of Phylomer® Peptides over Random Peptide Libraries

The Phylomer® Libraries compete directly against a panel of alternate peptide screening technologies, the most common being the random peptide libraries. Advantages of Phylogica’s Phylomers® over random peptide libraries include:

• Far better hit rate – Phylogica has obtained hit rates for peptides which are capable of disrupting protein interactions that are around 100 fold better than comparable hit rates obtained using random peptide screening technologies

• Higher stability – Phylomers® are derived from sub domains of natural proteins, which make them potentially more stable than conventional short random peptides.

• Greater structural diversity – Phylogica’s current Phylomer® library has a complexity of 50 million clones which is comparable with the numerical complexity of random peptide or antibody Fab fragment libraries. Phylomer® libraries represent diversity within all of the classes of protein scaffolds, while antibodies represent the structural diversity compatible with the one (antibody Fab) scaffold.

• Bio-informatic advantages – The source for Phylomers® are fully sequenced microbial genomes, which allows easy analysis of Phylomer hits.

Competitive Advantages of Phylomer® Peptides over other peptide libraries derived from biological genomes

Phylomers® are sourced from biological genomes that are not human in origin. This feature signifcantly enhances the potency associated with Phylomers® against human protein targets.

Many would argue that the origin of Phylomers® would also result in immunogenicity issues, however, the typical size of a Phylomer® ranges from 15-50 amino acids, which significantly reduces the probability of them containing immunogenic epitopes or cryptic motifs that could result in unintended interaction.

Phylomers® are capable of higher affinity binding (better fit) due to evolution selecting for intermediate affinities of interaction between proteins sourced from the same host species.