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Xeophin’s foundational IP is the cornerstone of our business, and central to everything that we do, and we take this very seriously. Our IP has been developed by the Founders Molloy and Neilson, and Xeophin has full worldwide exclusivity to exploit the IP. Along with this, patents are produced by FB Rice, and a full “Freedom to Operate” search has also been undertaken by FB Rice to ensure no unforeseen IP issues will arise, giving us a clear pathway ahead to market exclusivity for up to 32 years

 

Xeophin is currently undertaking genetic engineering to create a modified version of the TPV-2L protein (XeRA-1), derived from the Tanapox virus. This therapeutic will be a powerful Anti-TNF agent, acting on both TNF-a and TNFR1/R2, and is highly suitable for the treatment of Rheumatoid Arthritis (RA). This however is step one of an integrated four step plan for the use of XeRA-1, the remaining steps being:

  1. Genetic Engineering – Master the potential of XeRA-1
    protein as an immunotherapeutic;

  2. Oligonucleotide Interruption of Immune Response  – Forecast
    and overcome any long-term immunogenic response to XeRA-1
    (a problem shared by all current Anti-TNF therapies);

  3. Gene Therapy – Integrate XeRA-1 into the patient’s genome to
    create permanent, patient mediated TNF management;

  4. Therapeutic Gene Discovery Platform - Therapeutic Gene
    Discovery Platform – Continue to feed the pipeline with other
    XeRA-1 like genes

The combination of these four factors will result in ‘Mastery of TNF
Modulated Inflammation’ and a sustainable means to dominate the
RA market

Structure of 2L–TNFα. Disulfide bonds and ordered carbohydrates on 2L are shown as yellow sticks. The 2L–TNFα complex shown as a ribbon diagram in two orientations: looking down the three-fold symmetry axis (above) and with the three-fold axis vertical (middle). Below, a surface representation of TNFα from the complex structure, with the 2L-binding site highlighted in red at one of three interfaces on the TNFα trimer (TNFα subunits are different shades of blue).    Nat Struct Mol Biol . 2009 November ; 16(11): 1189.

Structure of 2L–TNFα. Disulfide bonds and ordered carbohydrates on 2L are shown as yellow sticks. The 2L–TNFα complex shown as a ribbon diagram in two orientations: looking down the three-fold symmetry axis (above) and with the three-fold axis vertical (middle). Below, a surface representation of TNFα from the complex structure, with the 2L-binding site highlighted in red at one of three interfaces on the TNFα trimer (TNFα subunits are different shades of blue).

Nat Struct Mol Biol. 2009 November ; 16(11): 1189.