Belharra’s Searchlight™ platform uses a photoaffinity‑based chemoproteomic library to map functional, non‑covalent binding pockets across the entire proteome in live cells. By combining high‑throughput mass spectrometry, bioinformatic analysis, and cellular screening, it delivers unbiased, proteome‑wide pocket discovery that supports pharmaceutical and biotech R&D in expanding target space for drug development.
Funding
$50M raised to dateRaised to date based on public sources. This may differ from the amount the company actually raised and is based only on what is publicly available on the internet.
Founders
Product
Problem
Many disease‑related proteins lack well‑characterized, druggable binding pockets, making them “undruggable” by conventional small‑molecule approaches. Existing chemoproteomics methods often rely on covalent probes that bias target selection and miss non‑traditional, transient sites, limiting the ability to discover novel therapeutics.
Solution
Belharra’s Searchlight™ platform uses a photoaffinity‑based chemoproteomic library that binds non‑covalently to proteins in their native cellular context, enabling unbiased detection of functional binding pockets across the entire proteome. The approach combines high‑throughput proteomics, advanced informatics, and cellular screening to map novel pockets on any protein or protein complex, regardless of cell type. Identified sites are linked to structural and functional data, facilitating downstream medicinal chemistry and drug development. By illuminating previously hidden pockets, the platform expands the targetable space for immunology, oncology, and other therapeutic areas, accelerating the discovery of first‑in‑class molecules.
Target Audience
Primary customers are pharmaceutical and biotech R&D teams seeking to expand their target space, particularly in immunology and oncology, as well as external partners requiring proteome‑wide pocket discovery for drug development.
Features
- Photoaffinity‑based library that probes non‑covalent, transient binding sites without bias toward cysteine residues
- Whole‑proteome screening in live cells, preserving native protein complexes and post‑translational modifications
- High‑throughput mass‑spectrometry workflow integrated with bioinformatic pipelines to annotate and prioritize novel pockets
- Ability to focus screens on specific proteins of interest or conduct unbiased, proteome‑wide surveys
- Generation of actionable hit lists that have been validated against historically “undruggable” targets
- Compatibility with downstream medicinal chemistry and structure‑based design workflows