Cutting-edge technologies for targeted research
At GRIDD, we have a variety of world-class technologies that help drive our research.
To access these technologies, or to explore them further, please contact us for more details.
Professor Quinn and his group have now used Magnetic Resonance Mass Spectrometry to investigate 62 potential protein targets for malaria using a natural-product-based fragment library. They found 96 low-molecular-weight natural products as binding partners of 32 of the putative malarial targets. Seventy-nine (79) fragments have direct growth inhibition on Plasmodium falciparum at concentrations that are promising for the development of fragment hits against these protein targets.
- State-of-the-art lab automation and high content imaging platforms
- Experienced assay development team, with a focus on HTS and HCI
- Hit discovery through to lead optimisation
- Expertise in optimising assay biology (adapting bench top assays to high throughput formats amenable for HTS)
- Biologically relevant parasite-based models suitable for HTS
- In-vitro 3D cancer cell models mimicking the tumour micro-environment, established in micro-titre plate format for HCI
- High-content phenotypic-based cellular screening
- Developing custom image analysis and scripting protocols.
FTMS use at GRIDD
Professor Sally-Ann Poulsen introduced FTMS use for the study of protein-ligand complexes to Australia, and was one of the first researchers worldwide, and the first in Australia, to utilise native state mass spectrometry to screen fragments by the direct observation of protein-ligand complexes. This approach holds significant promise in addressing the pipeline problems of the pharma industry.
Proteins are often the targets for drugs. One approach to discover new drugs is to identify chemicals, or small molecules, that interact with or bind to target proteins. Discovering which small molecules bind to a protein target is thus a critical first step in early-stage drug discovery. FTMS is a highly sensitive and unbiased approach that can be used to do just that— identify chemicals that bind to proteins.
How does it work? By “weighing” the protein before and after it is mixed with potential drug molecules. Imagine FTMS as a set of scales that measure (with exceptional accuracy) the mass of individual molecules. On the scales stands an elephant, representing a ‘heavy’ protein: the drug target. If a potential drug molecule binds to the protein, the FTMS detects an increase in mass of the ‘heavy’ protein because it has bound to a ‘very light’ drug molecule—like measuring the mass of an elephant holding an ice-cream. The FTMS instrument can differentiate this tiny mass difference—elephant empty-handed, versus elephant holding an ice-cream—and it is this tiny mass difference that provides the evidence needed to identify potential drug molecules.
- Expertise in native state mass spectrometry for intact protein analysis
- Initial assessment of the suitability of your protein target for fragment screening by native state mass spectrometry
- Fragment/small molecule screening campaign using native state mass spectrometry
- Qualitative and quantitative analysis of fragment/small molecule-protein binding
- High-resolution mass spectrometry analysis of small molecules.