Platform Introduction - Leads Biolabs

R&D

Antibody discovery and engineerin

Fully Human Phage Library
Adeptly screened several monoclonal and bispecific antibodies from our fully human phage library, many of which have progressed into clinical stage. This demonstrates the efficiency and effectiveness of our platform in identifying promising therapeutic candidates through rapid screening and selection.

Hybridoma Technology
For complex targets, we employ mouse hybridoma technology to generate a diverse pool of candidates. These candidates are subsequently refined through humanization technology, enhancing their therapeutic compatibility and effectiveness.

Alpaca Immune Library
Alpaca immune antibody library allows for the screening of both single-domain antibodies and alpaca IgG1 antibodies. Single-domain antibodies, being smaller and more stable than conventional antibodies, can recognize novel epitopes, offering improved penetration and accessibility to tumor tissues and microenvironments, which makes them highly effective in targeting difficult-to-reach areas.
In vivo and in vitro efficacy evaluation

Evaluating the in vivo and in vitro activities of antibody drugs is crucial during early discovery. Our pharmacology team, highly experienced in developing cell-based bioassays, has established a variety of stable cell lines and optimized a series of cell-based in vitro bioassays. Additionally, we have developed primary immune-cell assays tailored to the mechanism of action for each target. Our capabilities also include establishing a variety of humanized mouse models in-house for efficacy, pharmacodynamics, mechanism of action, and translational studies, as well as conducting preliminary toxicology and pharmacokinetic analyses.
Druggability assessment

We conduct comprehensive druggability assessments through a combination of software analysis, physical and chemical testing, immunoassays, accelerated tests and PK studies. By evaluating candidate molecules across multiple parameters, we identify and select lead molecules that meet stringent druggability requirements.
Proprietary technology platforms

Anchored by our deep understanding of molecular mechanism and disease biology, we have successfully developed a number of proprietary technology platforms geared towards different targets, mechanisms of action, and modalities. These technology platforms provide us with a broad arsenal of advanced tools and techniques for antibody design, screening and development, and empower us to engineer customized drug assets with high specificity in meeting underserved clinical demands across a wide spectrum of indications.
Our major technology platforms primarily include two T-cell engager platforms, the LeadsBody™ platform (a CD3 engager platform) and the X-body™ platform (a 4-1BB engager platform), as well as additional bispecific antibody and antibody fusion protein platforms.

LeadsBody™ platform (CD3 engager platform)
To achieve an optimal balance between the safety and efficacy of T-cell engagers, we have developed the proprietary LeadsBody™ platform, which facilitates diverse modifications to the molecular designs of CD3-targeted bispecific antibodies. These key modifications include, among others, variable expression levels in binding to tumor-associated antigens (TAA), fine-tuning CD3 affinity with differentiated cytokine release profiles, conditional T-cell redirecting and activation mechanisms within tumor microenvironments, and differing spatial structures. By harnessing this platform technology, our multiple CD3-targeted bispecific T-cell engaging antibodies for treating solid tumors and hematologic malignancies, such as LBL-034 and LBL-033, have demonstrated robust antitumor effects and favorable safety profiles in preclinical studies.

X-body™ platform (4-1BB engager platform)
X-body™ platform leverages advanced antibody engineering technology to create differentiated bispecific antibodies in a 2:2 format with high yield, high purity and excellent druggability. We have developed a method to enhance the yield and stability of the ScFv structure, which is applicable to most antibodies, allowing rapid conversion of Fab to ScFv.

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