Partner With Us
Current Out-Licensing Opportunities
VLST-007 (hCD47-hFc)
VLST-007 is a dimeric protein comprised of human CD47 extracellular domain fused to the Fc portion of a human IgG1 molecule. VLST-007 is designed to modulate the interaction between CD47 and its extracellular ligand, signal-regulatory protein a (SIRPα) CD47-Fc binding to SIRPα inhibits the activation of myeloid cells, which are important mediators of inflammation in autoimmune diseases VLST-007 is being developed as an inhibitor of inflammation for use in autoimmune and inflammatory conditions.
VLST has completed preclinical development of VLST-007, including in vitro and in vivo pharmacology studies, pilot pharmacokinetics and toxicology studies, and manufacturing scale up. We are actively seeking a partner for the continued development of this program.
VLST-002 (AntiKine Ab)
Chemokines are proteins that guide the migration of cells and play a key role in mediating inflammatory responses. Moreover, chemokines are implicated in numerous autoimmune and inflammatory diseases. The importance of chemokines in regulating leukocyte migration has been demonstrated in animal models where chemokine inhibition ameliorates symptoms of disease. We have generated and are humanizing a panel of antibodies reactive with multiple chemokines implicated in disease.
Early Discovery
VLST's proprietary platform technology has yielded over 70 virulence factor cellular target interactions to date including many suitable for targeting with a biologic therapeutic. In addition, many additional interactions have been identified which are suitable for targeting with small molecule therapeutics. These targets are available for both in-licensing and co-development opportunities.
Anti-Viral Target Discovery
VLST has applied its proteomics platform to identify host proteins that interact with HCV proteins, i.e., map the HCV viral protein-host protein interactome. Multiple novel and potentially drug-able targets have been identified. Disruption of viral-host protein-protein interactions provides a strategy for the development of new classes of HCV drugs. Targeting host proteins rather than viral proteins directly may have lower risk for acquired resistance than direct targeting of viral proteins. Additionally, known interactions have been identified supporting the validity of our findings. This proteomics approach to mapping viral protein-host protein interactomes is likely broadly applicable to other viruses such as HIV and influenza.
Inquiries
For additional information regarding VLST's partnering opportunities please contact:
Ron Myers
Vice President, Corporate Development & Legal Affairs
bd@vlstcorp.com