Robust proteome profiling of cysteine-reactive fragments using label-free chemoproteomics.

ABSTRACT: Identifying pharmacological probes for human proteins represents a key opportunity to accelerate the discovery of new therapeutics. High-content screening approaches to expand the ligandable proteome offer the potential to expedite the discovery of novel chemical probes to study protein function. Screening libraries of reactive fragments by chemoproteomics offers a compelling approach to ligand discovery, however, optimising sample throughput, proteomic depth, and data reproducibility remains a key challenge. We report a versatile, label-free quantification proteomics platform for competitive profiling of cysteine-reactive fragments against the native proteome. This high-throughput platform combines SP4 plate-based sample preparation with rapid chromatographic gradients. Data-independent a

SUBMITTER: Biggs GS 

PROVIDER: S-EPMC11697256 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature