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Condina, M. R.

Publications and source records attributed to Condina, M. R..

2 recordsLinked to original sources

Mass Dynamics 2.0: An improved modular web-based platform for accelerated proteomics insight generation and decision making

Data processing is essential to reliably generate knowledge from proteomics studies. The complexity of the proteomics data, as well as the ability of research teams to adopt complex analysis pipelines, have proven to be an obstacle to effective collaboration and more efficient biological insight generation. Here, we introduce MD 2.0, a cloud- and web-based platform for quantitative proteomics data, which implements a novel analysis workspace where statistical analyses, visualizations, and external knowledge generation are integrated into a modular framework. This modularity enables researchers the flexibility to test different hypotheses, and customize and template complex proteomics analyses, thereby expediting insight generation for complex datasets. The extensible MD 2.0 environment has been built with a scalable architecture to allow rapid development of future analysis modules and enhanced tools for remote collaboration, like experiment sharing and a live chat capability. The new drag-and-drop modules allow researchers to easily and quickly assess different aspects of an experiment, including quality control, differential expression and enrichment analysis. The modularity of MD 2.0 lays the foundation to support broader community-based analytical template generation and optimized sharing and collaboration between proteomics experts and biologists, thereby accelerating research teams abilities to extract knowledge from complex proteomics datasets.

bioinformatics↗

Magnetic Enrichment of Immuno-Specific Extracellular Vesicles for Mass Spectrometry Using Biofilm-Derived Iron Oxide Nanowires

Immuno-specific enrichment of extracellular vesicles (EVs) can provide important information into cellular pathways underpinning various pathologies and for non-invasive diagnostics, including mass spectrometry-based analyses. Herein, we report an optimised protocol for immuno-magnetic enrichment of specific EV subtypes and their subsequent processing with liquid chromatography-tandem mass spectrometry (LC-MS/MS). Specifically, we conjugated placental alkaline phosphatase (PLAP) antibodies to magnetic iron oxide nanowires (NWs) derived from bacterial biofilms and demonstrated the utility of this approach by enriching placental specific EVs (containing PLAP) from cell culture media. We demonstrate efficient PLAP+ve EV enrichment for both NW-PLAP and Dynabeads-PLAP, with high PLAP protein recovery (83.7{+/-}8.9% and 83.2{+/-}5.9%, respectively), high particle-to-protein ratio (7.5{+/-}0.7x109 and 7.1{+/-}1.2x109, respectively), and low non-specific binding of non-target EVs (7{+/-}3.2% and 5.4{+/-}2.2%, respectively). Furthermore, our optimized EV enrichment and processing approach identified 2518 and 2545 protein groups with LC-MS/MS for NW-PLAP and Dynabead-PLAP, respectively, with excellent reproducibility (Pearson correlation 0.986 and 0.988). These findings demonstrate that naturally occurring iron oxide NWs have comparable performance to current gold standard immune-magnetic beads. The optimized immunospecific EV enrichment for LC-MS/MS method provides a low-cost and highly-scalable yet efficient, high-throughput approach for quality EV proteomic studies.

bioengineering↗