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Bush, J. T.

Publications and source records attributed to Bush, J. T..

4 recordsLinked to original sources

Determinants of cysteine coverage by chemoproteomics

Covalent chemoproteomics has become a powerful route to expanding the druggable proteome, enabling proteome-wide screening of compounds that covalently modify nucleophilic residues, most commonly cysteine. Yet typical experiments detect only 5-18% of the ~250,000 cysteines encoded by the human proteome, and the determinants of this limited coverage remain poorlydefined. Here we combine cysteine featurisation, explainable machine learning (ML) and robust statistical filtering to establish what governs cysteine detectability in iodoacetamide- desthiobiotin (IA-DTB) chemoproteomics. Using a scalable feature-generation pipeline, we computed physicochemical and structural properties for cysteines and the corresponding tryptic peptides and trained models that predict detectability with high accuracy. Shapley analysis identifies protein abundance and intrinsic peptide properties governing LC-MS behaviour as the dominant determinants, whereas cysteine structural descriptors contribute comparatively little, indicating that detection is constrained downstream of probe reactivity. We further introduce a distance-based statistical filter that improves reproducibility across replicates, and show that cell line selection, subcellular fractionation and alternative electrophiles together expand coverage by >30%. More broadly, this work moves optimisation of chemoproteomics workflows from empirical trial-and-error towards rational, data-driven design.

bioinformatics↗

Efficient detection of cryptic pockets on challenging drug targets using MD-free co-vibrational modes

Allosteric and cryptic binding sites provide unique opportunities in drug discovery for achieving selectivity, reducing toxicity and unlocking challenging therapeutical targets. Yet, cryptic pockets are particularly elusive in that they are difficult to capture with experimental methodologies, and therefore often remain undetected. Computational approaches for flexible cryptic site detection traditionally involve extensive unbiased molecular dynamics simulations, or more efficient but computationally still highly demanding biased MD alternatives that make use of enhanced sampling along low-frequency motions of the protein structure. Here we utilize a new variant of the recently introduced and orders of magnitude faster, MD-free COVIB algorithm to identify cryptic pockets efficiently in two challenging targets, the KRAS oncoprotein and the N-terminal domain of the STAT5B transcription factor. Using experimental and AI-modelled structures, respectively, we identify numerous cryptic sites, some of which have not yet been reported. The sites are prioritized and validated with our pharmacophore optimized photoaffinity-tagged fragment library via MS-based peptide mapping and NMR spectroscopy. Besides identifying new, targetable regions on the surface of these important oncotargets, we have established a protocol combining COVIB-based cryptic pocket detection and photoaffinity-based experimental peptide mapping as a robust approach for exploring unique and tractable cryptic pockets.

biophysics↗

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

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 acquisition performed on a Bruker timsTOF Pro 2 consistently identified [~]23,000 cysteine sites per run, with a total of [~]32,000 cysteine sites profiled in HEK293T and Jurkat lysate. Crucially, this depth in cysteinome coverage is met with high data completeness, enabling robust identification of liganded proteins. In this study, 80 reactive fragments were screened in two cell lines identifying >400 ligand-protein interactions. Hits were validated through concentration-response experiments and the platform was utilised for hit expansion and live cell experiments. This label-free platform represents a significant step forward in high-throughput proteomics to evaluate ligandability of cysteines across the human proteome.

systems biology↗

A chemoproteomic platform for reactive fragment profiling against the deubiquitinases

Chemoproteomics is a powerful method capable of detecting interactions between small molecules and the proteome, however its use as a high-throughput screening method for chemical libraries has so far been limited. To address this need, we have further developed a chemoproteomics workflow to screen cysteine reactive covalent fragments in cell lysates against the deubiquitinating (DUB) enzymes using activity-based protein profiling. By using targeted ubiquitin probes, we have addressed sensitivity and affinity limitations, enabling target identification and covalent fragment library profiling in a 96-well plate format. The use of data independent acquisition (DIA) methods for MS analysis combined with automated Evosep liquid chromatography (LC) reduced instrument runtimes to 21 minutes per sample and simplified the workflow. In this proof-of-concept study, we have profiled 138 covalent fragments against 57 DUB proteins and validated four hit fragments against OTUD7B and UCHL3 through site identification experiments and orthogonal biochemical activity assays. Graphical abstract O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=93 SRC="FIGDIR/small/526632v1_ufig1.gif" ALT="Figure 1"> View larger version (19K): org.highwire.dtl.DTLVardef@2e036borg.highwire.dtl.DTLVardef@e27962org.highwire.dtl.DTLVardef@8f1caaorg.highwire.dtl.DTLVardef@1a3159a_HPS_FORMAT_FIGEXP M_FIG C_FIG

biochemistry↗