Technology

hyFc® Platform

hyFc® platform is our own proprietary technology designed to drive
the discovery of a wide range of differentiated agonistic protein therapeutics.

Based on one of leading long-acting technologies, hyFc® is designed to overcome the shortcomings of conventional IgG1 immunoglobulin-based Fc fusion proteins such as inflexible hinge which limits applicability and side-effects due to antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC).hyFc® is derived from non-cytosolic immunoglobulin IgD and IgG4 without site-directed mutagenesis. This gives flexible hinge that minimizes the loss of bioactivity of drug candidate and prevents adverse immunogenicity and cleavage by enzymes. hyFc® thus has broad applicability, less side-effects and superior long-acting characteristics to the drug candidates.

hyFc® Structure

hyFc® is a platform technology constructed to produce long-acting Fc fusion proteins by hybridizing IgD and IgG4

Human Ig Isotypes lgG1 lgG4 lgD
Hinge flexibility ++ + ++++
Binding of FcyR of
phagocytes (ADCC)		 ++++ ++ -
Activation of C1q (CDC) ++ - -
Binding of FcRn ++++ ++++ -
In vivo serum
half-life (days)		 21 21 3
  • Immunology Fifth Edition, by Kuby etc. p 90
  • J of Immunol. 1997 159: 3372
  • J of Immunol. 2004 172: 2925

hyFc® Strengths

Genexine's hyFc® technology can be applied to a broad range of drug moieties including small peptides and proteolytic enzymes. Genexine has a number of highly differentiated hyFc-based product candidates at various stages of development in its pipeline. We also have a undisclosed partnerships on hyFc® product candidates with leading biopharmaceutical companies.

  • Efficacy & Safety

    Higher bioactivity,
    no mutation,
    and low immunogenic risk

  • Long Half-Life

    Longer half-life
    than glycosylated products

  • Broad Application

    Applicable to cytokines, hormones,
    small peptides and Fab antibody

Publications

2015
  • Protective effects of Fc-fused PD-L1 on two different animal models of colitis. MY Song, CP Hong, SJ Park, JH Kim, BG Yang, Y Park, SW Kim, KS Kim, JY Lee, SW Lee, MH Jang and YC Sung. Gut. 2015, 64(2): 260-271
2014
  • Crucial Roles of Interleukin-7 in the Development of T Follicular Helper Cells and in the Induction of Humoral Immunity. YB Seo, SJ Im, H Namkoong, SW Kim, YW Choi, MC Kang, HS Lim, HT Jin, SH Yang, ML Cho, YM Kim, SW Lee, YK Choi, CD Surh, YC Sung. J Virol. 2014, 88(16): 8898-9009
2013
  • Controlled release of human growth hormone fused with a human hybrid Fc fragment through a nanoporous polymer membrane. ES Kim, DS Jang, SY Yang, MN Lee, KS Jin, HJ Cha, JK Kim, YC Sung, KY Choi. Nanoscale. 2013, 5(10): 4262-4269
  • The Pharmacology study of a new recombinant TNF receptor-hyFc fusion protein. JH Lee, JH Cho, JY, SH Lee, SH Yang, YC Sung, JH Kang, CS Park. Biologicals. 2013, 41(2): 77-83
  • Biochemical characterization of a new recombinant TNF receptor-hyFc fusion protein expressed in CHO cells. JH Lee, J Yeo, HS Park, G Sung, SH Lee, SH Yang, YC Sung, JH Kang, CS Park. Protein Expr Purif. 2013, 87(1): 17-26
2012
  • A Long-acting Erythropoietin Fused with Noncytolytic Human Fc for the Treatment of Anemia. SH Yang, SI Yang, YK Chung. Arch Pharm Res, 2012, 35(5): 757-759.
2011
  • Natural form of noncytolytic flexible human Fc as a long-acting carrier of agonistic ligand, erythropoietin. SJ Im, SI Yang, SH Yang, DH Choi, SY Choi, HS Kim, DS Jang, YK Chung, SH Kim, SH Paik, YC Park and YC Sung. Plos One. 2011, 6(9): e24574