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HCW Biologics’ Article Published in Cancer Immunology Research Validates Novel Tissue Factor Scaffold Fusion Protein (TOBI™) Discovery Platform
TOBI™ Discovery Platform Creates GMP-Scale Heteromeric Fusion Protein Complexes (HFPCs) That Solve Issues with Multi-Signal Receptor Engagement on Immune
About this update from Hcw Biologics Inc.
[{"type":"text","content":"TOBI™ Discovery Platform Creates GMP-Scale Heteromeric Fusion Protein Complexes (HFPCs) That Solve Issues with Multi-Signal Receptor Engagement on Immune Cells MIRAMAR, Fla., Aug. 17, 2021 (GLOBE NEWSWIRE) -- HCW Biologics Inc. (NASDAQ: HCWB), an innovative biopharmaceutical company, is focused on discovering and developing novel immunotherapies to lengthen health span by disrupting the link between chronic, low-grade inflammation and age-related diseases. The Company featured its internally-developed Tissue factOr-Based fusIon (TOBITM) discovery platform in a recent research article published online in the peer-reviewed journal Cancer Immunology Research. Using the TOBITM discovery platform, the Company has created novel multi-functional immunotherapeutics to rejuvenate the immune system to reduce the accumulation of senescent cells and suppress the activity of inflammasomes. These fusion immunotherapeutics are comprised of cytokines, chemokines, ligands, receptors, and single-chain antibodies carefully selected and designed to work in tandem to stimulate, inhibit, or target specific immune responses. The key aspect of the unique TOBITM platform is that it uses a novel tissue factor (“TF”) protein scaffold. The extracellular domain of human TF was selected as it has a rigid elongated structure comprised mainly of ß-sheets with its N- and C-termini located at distal ends of the polypeptide, permitting genetic fusions of other protein domains without anticipated steric interference. This TF domain does not interact with the cell membrane phospholipid bilayer and, as a result, does not exhibit procoagulant activity. Consistent with these properties, the Company found that genetic fusion to the TF domain promoted increased production of difficult-to-express proteins, such as IL-15. Additionally, the TF fusion proteins could be readily purified by affinity chromatography using anti-TF antibodies and low pH elution conditions, like those used in Protein A-based affinity purification of therapeutic antibodies. As a proof of concept, HCW Biologics’ published scientific article describes the creation of the molecules HCW9201 and HCW9207 as well as their individual functionality which mimic a cocktail of cytokines IL-12, IL-15, and IL-18 to prime memory-like natural killer (NK) cells for cell-based cancer therapy. However, use of the IL-...