Antibody discovery

TCE bispecific and trispecific antibodies

Antibody–cytokine fusion proteins

PROTiNB (proteolysis targeting intra-nanobody)

Antibody discovery

A world-leading antibody discovery platform combining various technologies to develope multifunctional antibodies and bioPROTACs.

Mouse hybridoma

Phage display

NGS

AI-powered drug design

Rabbit single B cell

FIND–cell surface display

Benefits

Single copy—connection between genotype and phenotype

Display of VHH, IgG and bsAb antibody structures

Identical post-translational modifications for better druggability

Cell surface display; high expression levels

Capacity up to 10E7

Applications

Significantly reduced time to lead compounds

Activity analysis during the high-throughput screening phase

Display and screening for multi-functional antibodies

Directed evolution—affinity maturation, druggability optimization, targeted mutagenesis

Discovery of antibodies with complex structures

NGS/AI-enabled drug development

TCE bispecific and trispecific antibodies

We innovate in the field of TCE antibodies with a platform leveraging anti-TCR/CD3 nanobodies,
enhancing efficacy through second signal and CD8 bias modifications,
and introduces the Fibody bispecific antibody design for improved druggability and therapeutic potential.

We develop a TCE platform with anti-TCR/CD3 nanobodies, instead of traditional anti-CD3 Fab/scFv, and avoid complex protein engineering.

Next-generation T-cell-engaging (TCE) trispecific antibodies with second signals/CD8 bias modifications demonstrate greater efficacy compared to traditional TCE bispecific antibodies.

Existing bispecific antibody technologies are facing challenges of druggability due to complex structures, or lack of general application due to reliance on VHH, scFv, etc.

Fibody is designed based on our early experience of fusion protein development. A receptor/ligand replaces CH1/CL of the antibody moiety to avoid light chain mispairing and retain the antibody conformation for greater druggability.

Antibody–cytokine fusion proteins

Due to its dimer structure, wild-type IL-10 causes toxicities leading to erythrocytopenia and thrombocytopenia, which limits its development and application. We use AI and molecular simulation software to optimize its structure and affinity. Side effects can be avoided even at high doses. Enriched at the target site via the antibody moiety, the engineered molecule exhibits improved anti-tumor efficacy.

Significantly limiting IL-10's ability to activate its receptors when in an unbound state

Enhancing IL-10's activation function when enriched at the target site via the antibody moiety

Significantly lowering toxicity in preclinical non-human primate studies

Bias modification of IL-10 to diminish immune-stimulatory functions for treating autoimmune diseases Demonstrating significant efficacy for treating tumors

PROTiNB (proteolysis targeting intra-nanobody)

Making undruggable targets druggable. While similar technologies are at their nascence, ours is at the global forefront, far surpassing others and demonstrating substantial potential.

Degrading undruggable targets (higher specificity than PROTACs)

Demonstrating superior safety profile thanks to the specific binding property of antibodies

Selecting E3 ligase from a wide range (wider than PROTACs), irrespective of the E3 expression levels at different sites; broad application enhanced by the ability to engineer the effector molecule