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What is proteomics?

Proteomics has evolved from a qualitative technique to a continuum of qualitative and quantitative using highly sensitive and accurate mass spectrometry to gain significant biological insights over a range of applications including biology, biochemistry, clinical/biomarker discovery and precision medicine.

Advances in protemoics have been led through increased sensitivity, dynamic range and throughput. With less sample than western blotting and no antibodies needed, modern quantitative mass spectrometry analyses can detect and quantify thousands of proteins in a single experiment across multiple conditions, with the dynamics analysed at a level that provides much greater understanding of how biological processes respond to different stimuli, or how they change within a cell, tissue, or organism over time, or while in a disease state. Importantly, proteins are preferred targets for therapeutic agents and diagnostic tests, with proteomics providing insights into the composition, functions, drug interactions, and regulation of proteins which are not predictable based on genome sequences.

Multiplexing proteomics

Advanced chemistry labelling tools, including tandem mass tags (TMT) have allowed multiplxing quantitation approaches to comprehensively identify and quantify proteins, sensitively detect rare peptide species, identify differences between healthy and diseased states, and conduct sophisticated surveys of the cellular proteome. We employ TMT labelling and other multiplexing approaches for these significant advantages in current proteomic workflows

Signalling proteomics (phosphorylation)

Phosphorylation is a critical protein post-translational modification that can modulate protein activity, abundance, interaction, and localisation. Recent advances in enrichment workflows and mass spectrometry instrumentation have led to the development of powerful methods for proteome-wide phosphorylation analysis in complex biological samples, including cells, cell organelles, and tissues. We also investigate other protein- and lipid-based modifications.

Translational proteomics

Translational research is accelerating the conversion of basic scientific knowledge into tests, treatments and practices that improve human health. Recent advances in sample preparation and mass spectrometry have increased capabilities in using proteomics to direct insights into complex biological systems, impacting our understanding of health and disease. Often employing nano-scale sample types (tissue, biopsy, biofludis), translational proteomics complements other omics disciplines (genomics, transcriptomics, and metabolomics/lipidomics), delivering new workflows to generate clinically relevant data that are quantitative, reproducible, standardised, and scalable.

Proteomics research at the Baker Institute

Here at the Baker Institute, our investigators use protein chemistry, subcellular fractionation, sensitive enrichment and sample preparation strategies, with mass spectrometry and informatic analyses, to understand the composition, expression, interactions, protein modifications, and signalling dynamics of proteins in health and disease.

In the context of heart physiology, this allows unique insights into heart composition and function, and discover proteins and their modifications in cell types/systems previously undefined. Importantly,, this helps to identify dysregulated protein networks and previously unrecognised pathways in heart disease and discover potential targets for diagnosis, therapeutic intervention, or monitoring. Importantly, proteomics provides important insights into our understanding of cell signalling — specifically the quantitative identification of protein cargo and biological insights of extracellular vesicles (including exosomes) — key intercellular communicators affecting gene expression and phenotype in target cells.

For more information, contact:

David Greening
Lab Head, Molecular Proteomics
Head of the Proteomics Research Platform
E: david.greening@baker.edu.au

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