The synthesized GLP-1R / GIPR dual agonist is coupled with fatty acid chain. The proportion of GLP-1R and GIPR activity is the best after a lot of screening. In preclinical animal experiments, DR10627 showed extremely significant hypoglycemic and weight-loss effects. Indications include diabetes, obesity and other metabolic diseases.
Based on the Multiplebody ® platform, DR10624 is designed as a tri- activity human Fc fusion protein，characterized by GLP-1 / GCG dual activity and FGF21 activity. DR10624 is expected for the treatment of metabolic diseases such as diabetes, obesity and nonalcoholic fatty liver (NASH).
Based on the Multiplebody ® platform, DR10625 is designed as a tri- activity human Fc fusion protein，characterized by GLP-1 / GIP dual activity and FGF21 activity. DR10625 is expected for the treatment of metabolic diseases such as diabetes, obesity and nonalcoholic fatty liver (NASH).
Claudin 18.2 (CLDN18.2) is specifically expressed in highly differentiated normal gastric mucosa, but also in gastric and pancreatic cancer. Due to the tight adhesion between cells, it is very difficult for antibody drugs to bind to normal tissues. However, the loose structure of the interstitial space of cancer cells makes CLDN18.2 possible to be exposed to macromolecular protein drugs, so CLDN18.2 is an ideal target for a new generation of anti-tumor therapy. DR30303 is a fusion protein composed of single domain antibody and human Fc and specifically recognizes the of CLDN18.2. It has a killing effect on CLDN18.2 positive tumor cells through ADCC and CDC. At the same time, due to the characteristics of the target, it also reduces the toxicity to normal CLDN18.2 positive tissues. It is intended to be used in the treatment of gastric cancer and other solid tumors with abnormal expression of CLDN18.2.
DR30310 is a tri-specific fusion protein composed of anti-CLDN18.2 single domain antibody, anti-HSA single domain antibody and anti-CD3e scFv. In vitro, DR30310 showed a strong T cell mediated killing effect. It is a potential new generation of anti-tumor drugs.
The long-acting human hyaluronidase (PH20) based on xlongylation ® platform is used to decompose hyaluronic acid (HA) in tumor microenvironment, reduce the fluid pressure of tumor stroma, improve the killing efficiency of immune system to tumor tissue, and promote the permeability of drugs to tumor tissue.
DR30207 is designed as a tri-specific antibody of anti- PDL1 / XXXX / XXXX based on MultipleBody® platform. it can simultaneously antagonize three targets ——PDL1, XXXX and XXXX, has dual effects of inhibiting neovascularization and relieving immunosuppression. It is intended to be used in the treatment of diverse solid tumors.
DR50402 is designed as a IL-15/IL-15RaSushi fusion protein based on Accubody® platform and xLONG® platform. High hydrophilic xlong ® sequence makes the hydration radius of DR50402 reach the nanometer level, then EPR effect is formed in vivo, which is conducive to the enrichment of tumor tissue; xlong ® sequence is connected with IL15/IL15RaSushi through a specific enzyme cutting site, and xlong ® sequence is removed through a specific protease at the tumor site, which recover the binding ability to IL-15Rβγ. Compared with IL-15, due to the pre binding of α receptor subunits, IL-15/ IL15RaSushi (IL-15 superagonist) has enhancing affinity to IL-15Rβγ widely expressed on NK cells and CD8 + memory T cells, and so stimulates the proliferation of NK cells and activated T cells.
DR30121 is developed as an ultra-long acting anti-VEGF / Ang-2 dual antagonist for angiogenic ophthalmic diseases such as AMD and DMD based on the multiplebody ® and xlongylation ® platform. VEGF binding region and angiopoietin-2 (Ang-2) binding region were fused in the N-terminal and C-terminal of human Fc respectively. In order to further increase the hydration radius, another xlong ® sequence was introduced in the N-terminal of VEGF binding region, which give DR30121 an extra-long vitreous half-life.
DR10112 is developed as the human growth hormone (hGH) fusion protein based on the xlongylation ® platform. The anti-HSA single domain antibody was fused with hGH at the N-terminal, which prolongs the half-life in vivo. The xlong ® sequence was fused with hGH at the C-terminal, which reduces the binding ability between hGH and receptor, and weakens the clearance mediated by GH receptor.