Anti-CD28 VHHs for Trispecific T Cell Engagers in Cancer Therapy

A study by Hui Wang isolated 34 VHHs (nanobodies) from a phage-display library using PBMCs of an immunized Bactrian camel. These VHHs bind to the human CD28 protein with EC50 values from 8.5 nM to 130 nM and were evaluated for co-stimulatory activity in trispecific T cell engagers targeting DLL3, CD3, and CD28. The dataset, last updated on 2026-04-17, contains results from affinity screening, functional ranking, and therapeutic efficacy evaluation.

Use Cases

• Ranking antibody candidates based on EC50 binding values ranging from 8.5 nM to 130 nM.
• Evaluating the co-stimulatory activity of anti-CD28 VHHs when incorporated into trispecific T cell engagers.
• Comparing tumor-specific cytotoxicity of trispecific engagers (targeting DLL3, CD3, CD28) to bispecific engagers.
• Structural mapping of antibody-epitope interactions, such as the CD28 epitope involving residues Arg34, Tyr51, and Tyr61.

Strengths

• Includes data on 34 distinct VHH candidates, providing a panel for comparison.
• Reports specific quantitative binding metrics (EC50 values) for each VHH.
• Contains functional evaluation data from integrated screening, ranking, and therapeutic efficacy tests.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• The 4.8 MB file size suggests a relatively small dataset.

Provenance

Source

figshare

Collection Method

Data generated from phage-display screening of an immune library, followed by affinity and functional assays.

Freshness

Last updated 2026-04-17 05:22:13; freshness should be verified.