HCW Biologics’ Founder and CEO Dr. Hing C. Wong Participating in Cambridge Healthtech Institute’s Annual PepTalk Conference 2022

A Novel Platform to Create Multi-Functional Immunotherapeutics for Cancer Will Feature TOBI Discovery Platform and Lead Product Candidate, HCW9218

MIRAMAR, Fla., Jan. 19, 2022 (GLOBE NEWSWIRE) -- HCW Biologics Inc. (“HCW Biologics” or the “Company”) (NASDAQ: HCWB), a biopharmaceutical company focused on discovering and developing novel immunotherapies to lengthen health span by disrupting the link between chronic, low-grade inflammation and age-related diseases, today announced that Hing C. Wong, Ph.D., Founder and CEO of HCW Biologics, will speak at the Cambridge Healthtech Institute’s 24^th Annual PepTalk Conference to be held on January 17-19, 2022 (https://www.chi-peptalk.com/protein-expression-production). The conference is taking place virtually and in person at the Hilton San Diego Bayfront in San Diego, California.

Dr. Wong’s presentation entitled, “A Novel Platform to Create Multi-Functional Immunotherapeutics for Cancer,” is part of the session for Recombinant Protein Expression and Production: Effective Expression and Production of Unique Bioproducts and takes place on January 19 at 11:15 a.m. PST. His presentation will feature a discussion of the Company’s internally developed platform for drug discovery called the TOBI (Tissue factOr-Based fusIon) platform. The TOBI platform is a scaffold for the creation of novel multi-functional immunotherapeutics that have the potential to rejuvenate the immune system by reducing the accumulation of senescent cells and suppressing the activity of inflammasomes. Using the TOBI platform, the Company has developed over 30 molecules that are capable of activating and targeting desired immune responses and blocking unwanted immunosuppressive activities.

Dr. Wong stated, “The TOBI platform is a novel approach to construct multi-functional fusion proteins and fusion protein complexes, all components are human-derived, using a novel tissue factor (TF) 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. It is expressed at high levels by most cell types and is not expected to be immunogenic in humans.”