SCIENCE

T-sphaeraᵀᴹ

T-sphaera Platform for Drug Innovation

We are developing a next-generation protein drug platform, T-sphaera, based on Apoferritin (the iron-free form of ferritin*). Apoferritin has a naturally stable nanoparticle structure, which we engineer to enhance its therapeutic potential as a targeted functional protein. Leveraging this innovative platform, we are committed to developing precise and effective anticancer therapeutics, aiming to provide superior treatment options for patients.

* Ferritin is a globular, nanometer-scale protein that plays a crucial physiological role in the human body by storing and releasing iron (Fe) as needed. It is widely distributed across various tissues and interacts with specific cellular receptors, making it a biologically important and versatile molecule.

* Ferritin is a globular, nanometer-scale protein that plays a crucial physiological role in the human body by storing and releasing iron (Fe) as needed. It is widely distributed across various tissues and interacts with specific cellular receptors, making it a biologically important and versatile molecule.

Key Characteristics of T-sphaera

  • · Three-dimensional nanosphere formed by self-assembly of 24 subunits
  • · Uniform and hollow spherical structure with diameter of approximately 12 nm
  • · Highly stable structure that remains intact under elevated temperature (40-60℃) and broad pH range (pH 4-10)
  • · Ideal biomaterial platform due to its ability to retain structural integrity even after surface display of antigens, peptides, or other functional proteins

T-sphaera : A Cutting-Edge Plug-and-Play Platform for Drug Development

Our core technology, T-sphaera, is a spherical protein composed of 24 identical subunits derived solely from the heavy chains of native human ferritin. To reduce undesired binding to the transferrin receptors, we introduced specific mutations that diminish its affinity for these receptors. On this optimized T-sphaera Platform, we graft various binding epitopes—such as antibody-derived CDRs, functional peptides/domains—onto multiple surface regions, including the N-terminus, C-terminus, and loop regions. This modular engineering enables rapid and flexible incorporation of diverse targeting moieties, making T-sphaera a plug-and-play therapeutic platform adaptable to various targets and disease indications. As a result, T-sphaera can function as a targeted anti-cancer therapeutic with antibody-like binding properties, while maintaining the low immunogenicity inherent to human-derived proteins.

Key Advantages of T-sphaera-based
Drug Development Platform

1

Modular Plug-and-Play Platform

T-sphaera is a versatile platform with high flexibility, allowing for the easy discovery of diverse therapeutics by simply grafting functional domains such as antibody CDRs, peptides, or ligands onto the surface of T-sphaera.

2

Multivalent Binding for Easy Targeting

The 24-mer structure of T-sphaera provides 24 antigen-binding sites, enabling strong multivalent interactions which are especially advantageous for targeting cells with low antigen expression.

3

Low Immunogenicity & Excellent Biocompatibility

As a human-derived nano-biomaterial, T-sphaera exhibits minimal immunogenicity and low risk of side effects offering a favorable safety profile for clinical development.

4

High Structural Stability & Various Expression Systems

T-sphaera’s robust nanostructure supports diverse conjugation strategies (e.g., ADCs), and we leverage the efficiency of E. coli expression for faster and more cost-effective development. For the commercial development, we have flexibility in utilizing either E. coli or CHO systems depending on the optimal path forward.

T-sphaera Characterization

*TfR: Transferrin Receptor

Possible Binding Sites and Binding Ratios

Binding Sites Target Binding Ratios (Illustrative)

Cell Binding Capacity

Target-specific Binding Profiles Expression Level of Target Over-expressed Cell > 50%
Cancer Cell: A375, PD-1 Effector Cell, A375
Concentration: 100 nM
Expression Level of Target Low-expressed Cell < 1%
Cancer Cell: A375sm, NK92MI, MDA-MB-468
Concentration: 100 nM
  • · T-Sphaera binding varies depending on target structure, epitope properties, and 3D folding.
  • · Epitope spacing on 24-mer surface is considered to minimize binding hindrance in drug design.
  • · Despite low target expression, T-Sphaera shows similar binding patterns due to its 24-mer structure and high avidity, which is a key advantage of the platform.
PD-L1 Low Cancer Cell (A375sm)
In PD-L1 low-expressing cell lines, our bi-specific candidates
demonstrated superior binding affinity compared to the antibody.

Harnessing our T-sphaera platform technology, we are developing two distinct therapeutic approaches.

Our first approach focuses on the development of single or multi-target oncology therapeutics. Multi-target oncology therapeutics offer functional advantages over conventional antibodies by engaging two distinct targets simultaneously. This allows for the modulation of multiple signaling pathways involved in tumor growth and immune evasion and/or the physical bridging of immune and tumor cells to enhance anti-tumor activity. Through this mechanism, we aim to achieve improved specificity, increased efficacy, and more durable therapeutic responses.

Our second approach focuses on drug conjugates, a breakthrough modality designed to overcome the limitations of traditional therapies. By striking the perfect balance between higher tumor selectivity for precise targeting and the potent anti-cancer efficacy of cytotoxic payloads, we are developing next-generation drug conjugates.

Multi-target Therapy Drug Conjugation