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Serrano, L. R.

Publications and source records attributed to Serrano, L. R..

5 recordsLinked to original sources

Improving Generalizability in Whole-Cell Antibiotic Discovery Through Active Learning

Machine learning (ML) has accelerated molecular discovery, yet training models to generalize to out-of-distribution (OOD) chemical spaces remains fundamentally constrained by the high cost of experimental validation. In antibiotic discovery, where whole-cell phenotypic high throughput screening (HTS) is resource-intensive, iterative ML-guided compound selection - or Active Learning (AL) - offers a pathway to efficiently navigate available chemical spaces. However, the algorithmic tradeoffs between prioritizing compound novelty (exploration), predicted bioactivity (exploitation), and their impact on OOD generalizability remain unresolved for noisy, whole-cell biological systems. In this work, we systematically evaluate three AL strategies for whole-cell bacterial bioactivity and benchmark their effects on model accuracy, hit rate, and OOD performance. Using retrospective simulations on Mycobacterium tuberculosis HTS data, we identify an optimal AL strategy that balances predicted hit/non-hit novelty with overall hit rate. We then integrate the strategy in a closed-loop Borrelia burgdorferi antibiotic discovery HTS campaign. The AL-guided approach successfully increased the experimental screening hit rate five-fold (from a 0.2% rate within investigator-selected plates to 1.0%). Further, when the trained model was applied in prospective in silico selection of highly diverse compounds across multiple bacterial species, the AL-trained whole-cell inhibition predictor demonstrates 53-fold enrichment over investigator-directed screening (11.0% experimental validation of predicted hits). Of these, 100% demonstrated the intended narrow spectrum activity for Borrelia burgdorferi. These results demonstrate that calibrated AL strategies can overcome data acquisition bottlenecks and train generalizable property predictors able to extrapolate to OOD molecules.

bioinformatics↗

Rapid Peptide Mapping of Monoclonal Antibodies with Direct Infusion Mass Spectrometry

Peptide mapping is a critical tool for characterizing biotherapeutic proteins and is essential for the development of monoclonal antibody drugs. Here we describe a new direct infusion technology that streamlines peptide mapping data collection and analysis, accelerating the method by up to 100-fold. This method, which we term RaPiD-mAb-MS, combines high-throughput plate-based sample preparation with direct infusion mass spectrometry analysis. RaPiD-mAb-MS allows analysis of 96 samples within [~] 1.5 to 2 hours, routinely achieves >95% sequence coverage, and has been successfully applied to 28 unique antibodies and over 2,000 samples. Here we demonstrate that RaPiD-mAb-MS detects and quantifies oxidation, deamidation, isomerization, glycosylation, and sequence variants with results comparable to conventional LC-MS based methods in a fraction of the time. Further, by eliminating chromatography, data analysis is greatly streamlined and simplified. By allowing for the collection of [~] 1,000 peptide maps per day, RaPiD-mAb-MS is positioned to accelerate all phases of antibody-based drug discovery & development and sets the stage for collection of massive datasets that would allow artificial intelligent prediction of optimal antibody variants and formulations.

biochemistry↗

SPE-CZE-MS quantifies zeptomole concentrations ofphosphorylated peptides

Capillary zone electrophoresis (CZE) is gaining attention in the field of single-cell proteomics for its ultra-low-flow and high-resolution separation abilities. Even more sample-limited yet rich in biological information are phosphoproteomics experiments, as the phosphoproteome composes only a fraction of the whole cellular proteome. Rapid analysis, high sensitivity, and maximization of sample utilization are paramount for single-cell analysis. Some challenges of coupling CZE analysis with mass spectrometry analysis (MS) of complex mixtures include 1. sensitivity due to volume loading limitations of CZE and 2. incompatibility of MS duty cycles with electrophoretic timescales. Here, we address these two challenges as applied to single-cell equivalent phosphoproteomics experiments by interfacing a microchip-based CZE device integrated with a solid-phase-extraction (SPE) bed with the Orbitrap Astral mass spectrometer. Using 225 phosphorylated peptide standards and phosphorylated peptide-enriched mouse brain tissue, we investigate microchip-based SPE-CZE functionality, quantitative performance, and complementarity to nano-LC-MS (nLC-MS) analysis. We highlight unique SPE-CZE separation mechanisms that can empower fit-for-purpose applications in single-cell-equivalent phosphoproteomics.

systems biology↗

One-Hour Phosphoproteome Analysis with the Orbitrap Astral Mass Spectrometer

Owing to its roles in cellular signal transduction, protein phosphorylation plays critical roles in myriad cell processes. That said, detecting and quantifying protein phosphorylation has remained a challenge. We describe the use of a novel mass spectrometer (Orbitrap Astral) coupled with data-independent acquisition (DIA) to achieve rapid and deep analysis of human and mouse phosphoproteomes. With this method we map approximately 30,000 unique human phosphorylation sites within a half-hour of data collection. The technology was benchmarked to other state-of-the-art MS platforms using both synthetic peptide standards and with EGF-stimulated HeLa cells. We applied this approach to generate a phosphoproteome multi-tissue atlas of the mouse. Altogether, we detected 81,120 unique phosphorylation sites within 12 hours of measurement. With this unique dataset, we examine the sequence, structural, and kinase specificity context of protein phosphorylation. Finally, we highlight the discovery potential of this resource with multiple examples of novel phosphorylation events relevant to mitochondrial and brain biology.

systems biology↗

Pptc7 maintains mitochondrial protein content by suppressing receptor-mediated mitophagy

Pptc7 is a resident mitochondrial phosphatase essential for maintaining proper mitochondrial content and function. Newborn mice lacking Pptc7 exhibit aberrant mitochondrial protein phosphorylation, suffer from a range of metabolic defects, and fail to survive beyond one day after birth. Using an inducible knockout model, we reveal that loss of Pptc7 in adult mice causes marked reduction in mitochondrial mass concomitant with elevation of the mitophagy receptors Bnip3 and Nix. Consistently, Pptc7-/- mouse embryonic fibroblasts (MEFs) exhibit a major increase in mitophagy that is reversed upon deletion of these receptors. Our phosphoproteomics analyses reveal a common set of elevated phosphosites between perinatal tissues, adult liver, and MEFs-- including multiple sites on Bnip3 and Nix. These data suggest that Pptc7 deletion causes mitochondrial dysfunction via dysregulation of several metabolic pathways and that Pptc7 may directly regulate mitophagy receptor function or stability. Overall, our work reveals a significant role for Pptc7 in the mitophagic response and furthers the growing notion that management of mitochondrial protein phosphorylation is essential for ensuring proper organelle content and function.

biochemistry↗