Phylogica Peptide Fusion Kills Aggressive Breast Cancer Cells
A pilot study by Associate Professor Pilar Blancafort, a member of the Harry Perkins Institute of Medical Research, shows that Phylogica’s cell penetrating peptides (CPPs) linked with the Omomyc drug kill aggressive drug resistant breast cancer cells in vivo.
Professor Blancafort also observed that Phylogica’s CPP fusion significantly improved the efficacy of existing anticancer drugs including the antibody Cetuximab and the chemotherapy agent Docetaxel. For example, a combination of Cetuximab and a Phylomer CPP-Omomyc fusion was more than three times more effective at killing drug resistant breast cancer cells than either of these agents alone.
Associate Professor Blancafort commented: “The ability to combine drugs to treat breast cancer is particularly exciting as it has the potential to lower the likelihood of resistance, improve drug activity and reduce chemotherapy side-effects.”
In a final pilot study, Associate Professor Blancafort tested the activity of Phylogica’s CPP fusion in an in vivo breast cancer model. A substantial reduction in tumour size was observed in tumours injected with Phylogica’s CPP fusion when compared to controls. This pilot study needs to be repeated using larger groups to confirm its significance.
Dr Paul Watt, Chief Scientific Officer of Phylogica said: “We were not expecting such a striking result from the pilot study. We believe this is the first time anyone has shown a CPP-Omomyc fusion protein to be active in vivo, as to our knowledge Omomyc has only previously been successfully delivered to tumours using a complex ‘gene therapy’ approach, associated with significant regulatory hurdles to clinical application.”
Phylogica’s CEO, Dr Richard Hopkins noted: “The ability of Phylogica’s delivery system to kill cancers from the inside and improve the efficacy of existing drugs is a potential paradigm shift for cancer therapeutics because it opens up the intracellular target landscape to next generation biologics drugs such as proteins.”
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