School of Science

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Food Science

Our Research Interests

Our primary research vision is to oversee the adoption of innovative, next generation proteomics tools and workflows that enable the delivery of excellent science and impact for ECU and its partners. In the post-genomics era, proteomics and mass spectrometry (MS) can validate the predictions made by genomics/transcriptomics, but moreover can identify key proteins involved in regulating biological systems.

At ECU Proteomics, we use MS to undertake fundamental and translational research including biomarker identification and the creation of diagnostic tools. The proteomics group at ECU has vast experience in the application of proteomics technology to the food and agricultural sciences, as well as expertise in proteomics bioinformatics, transcriptomics and computational systems biology.

Our research program focuses on understanding grain biochemistry (in field and during food processing), changes in protein expression under biotic and abiotic stress conditions and the role of grain proteins in food intolerance.

What is LC-MS proteomics?

Liquid chromatography-mass spectrometry (LC-MS) enables peptide separation, typically by reversed phase HPLC, followed by mass analysis using mass spectrometry (MS). At ECU, we are using bottom-up (or shotgun) proteomics for protein identification and quantitation. Proteomics can also be used for protein characterisation through both sequence and post-translational modification analysis.

How can researchers use proteomics?

Protein identification

Modern proteomics experiments can identify thousands of proteins in a single experiment. In bottom-up proteomics, we employ enzymes (e.g. trypsin) to first digest the proteins in a mixture to yield peptides that are then separated and analysed by LC-MS.

Protein quantitation

At ECU, we use two quantitative strategies: relative and absolute quantitation. We use data-independent acquisition (DIA) to perform label-free quantitation of thousands of proteins using the SWATH-MS technology. Additionally, we use the multiple reaction monitoring (MRM) MS targeted quantitation strategy for relative protein quantitation, or we use paired heavy/light peptide standards to achieve absolute quantitation.