Our Advanced Technologies
Nucleotide Enzymatic Synthesis Technology
2'-fluorinated nucleosides refer to nucleoside derivatives which the hydroxyl group at the 2'-position of the ribose ring is replaced by a fluorine atom, including 2'-fluoro-2'-deoxyuridine, 2'-fluoro-2'-deoxycytidine, 2'-fluoro-2'-deoxyadenosine and 2'-fluoro-2'-deoxyguanosine. The phosphoramidites synthesized using these as substrates are widely used in the production of small nucleic acid drugs (e.g., ASO, siRNA, aptamers) and antiviral/anticancer nucleoside-based drugs. Introducing 2'-fluorinated nucleosides can enhance nuclease resistance, improve target RNA binding affinity, optimize pharmacokinetics (prolonging half-life), while maintaining Watson-Crick base pairing capability. 2'-fluoro-2'-deoxyuridine and 2'-fluoro-2'-deoxycytidine can be synthesized chemically with relative ease, whereas the chemical synthesis of 2'-fluoro-2'-deoxyadenosine and 2'-fluoro-2'-deoxyguanosine involves numerous steps and low yields. Through the discovery and modification of novel enzymes, we achieved the enzymatic conversion of 2'-fluoro-2'-deoxyuridine to 2'-fluoro-2'-deoxyadenosine in a single step and to 2'-fluoro-2'-deoxyguanosine in two steps, with high conversion rates and simple purification, enabling large-scale production (hundreds of kilograms) and significantly reducing costs.
GalNAc Biosynthesis Technology
D-galactosamine (D-GalNH2) is chemically named 2-amino-2-deoxy-D-galactose and is often found in the form of hydrochloride salt. At present, the most commonly used preparation method is acid hydrolysis of chondroitin sulfate, and then purified by strong acid cationic resin. This process uses a large amount of acid and base, which can cause environmental pollution. More importantly, chondroitin sulfate is generally extracted from animal cartilage, and there is a risk of animal virus contamination. Through metabolic engineering of microorganisms and introducing exogenous synthetic pathways, we have pioneered a fermentation-based synthesis technology for non-animal source D-galactosamine. After simple purification, product with HPLC-ELSD purity more than 99% and endotoxin < 50EU/g was obtained. The whole process is green and environmentally friendly, and GMP grade is available.
ADC and AOC Glyco Site-Specific Conjugation Technology
Antibody–drug conjugates (ADCs) combine the targeting ability of monoclonal antibodies with the potency of cytotoxic drugs. Traditional conjugation methods often yield heterogeneous mixtures with varying drug-to-antibody ratios (DARs), which can affect efficacy and safety. Site-specific glycan conjugation is an advanced approach that leverages the natural glycosylation sites in the Fc region of antibodies. By enzymatically remodeling these glycans, drug payloads can be attached at defined positions with high uniformity.
Synaffix GlycoConnectTM Technique
GlycanLink DisacLinkTM Technique
Glycogene developed α-2,3 sialyltransferase catalyzed site-specific glycan conjugation method, which showed better batch-to-batch consistency, wider therapeutic window and reduced systemic toxicity. This technology uses human-derived α2,3 sialyltransferase to transfer azide-modified sialic acid at the 5th or 9th position to the terminal of antibody glycans. Subsequently, toxin molecules are site-specifically conjugated to the terminal of antibody glycans through a one-step click chemistry reaction, successfully achieving site-specific conjugation with DAR values controllable around 4 and 2. This technology has been granted a patent, with patent number ZL 2025 1 1814151.5.
AOC Glyco Site-Specific Conjugation Technology is an advanced platform that enables precise attachment of cytotoxic payloads to the conserved Fc glycan (Asn297) of monoclonal antibodies via chemoenzymatic remodeling and bioorthogonal click chemistry. It generates highly homogeneous AOCs with a defined DAR , preserving antibody structure and antigen affinity without genetic engineering. This technology enhances stability, reduces premature payload release and off-target toxicity, improving pharmacokinetics and antitumor efficacy for next-generation targeted therapeutics.
GlycoADC Platform
Chemical linkers in antibody drug conjugates play crucial roles in delivery of cytotoxic drugs into cancer cells to ensure target-responsive release of active therapeutic format. However, hydrophobic payloads often induce ADC aggregation and resist high drug antibody ratio (DAR), leading to rapid in vivo clearance and compromised therapeutic effects.
Glycogene developed Sialyl Lewis X modified linker (i.e., GlycoADC), which can improve the hydrophilicity significantly. Furthermore, it could enhance the tumor regression and serum stability dramatically.
