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Infrared (IR) imaging technology at the Australian Synchrotron, developed specifically for carbon fibre analysis, has contributed to a better understanding of chemical changes that affect structure in the production of high-performance carbon fibres using a precursor material.
A research collaboration led by Carbon Nexus, a global carbon fibre research facility at Deakin University, Swinburne University of Technology and members of the Infrared Microspectroscopy team at the Australian Synchrotron, has just published a paper in the Journal of Materials Chemistry A, that identified and helped to explain important structural changes that occur during the production of carbon fibres.
The research was undertaken to elucidate the exact chemical transformation occurring during the heat treatment of polyacrylonitrile (PAN), which produced structural changes.
Left to right: Nishar Hameed, Maxime Maghe and Srinivas Nunna on the Australian Synchrotron Infrared Spectroscopy beamline.
The majority of commercial carbon fibres are manufactured from PAN but there has been an imperfection that occurred during production that affected its material properties.
Because the conversion of PAN to carbon fibre did not occur evenly across the fibre, it resulted in a skin-core structure.
Manufacturers want to prevent the formation of the skin-core structure in order to enhance the strength of the fibres.
The research lead by Dr Nishar Hameed provides the first quantitative definition on the chemical structure development along the radial direction of PAN fibres using high-resolution IR imaging.
“Although it has been more than half a century that carbon fibres were first developed, the exact chemical transformations and the actual structure development during heat treatment is still unknown”.
“The most significant scientific outcome of this study is that the critical chemical reactions for structure development were found to be occurring at a faster rate in the core of the fibre during heating, thus disrupting the more than 50-year-old belief that this reaction occurs at the periphery of the fibre due to direct heat.”
A multitude of experimental techniques including IR spectroscopy confirmed that structural differences evolved along the radial direction of the fibres, which produced the imperfection.
The difference between skin and core in stabilised fibres evolved from differences in the cross linking mechanism of molecular chains from the skin to the core.
The information could potentially help manufacturers improve the production process and lead to better fibres.
“Using a technique called Attenuated Total Reflection (ATR) to focus the synchrotron beam, the IR beamline allowed the research team to acquire images across individual fibres, to see where carbon-carbon triple bonds in the PAN were being converted to double bonds,” said Dr Mark Tobin, Principal Scientist, IR, at the Australian Synchrotron, who is a co-author with Dr Pimm Vongsvivut and Dr Keith Bambery.
“Previous IR studies have been conducted on fibre bundles and powdered fibres, while we were able to analyse the cross section of single filaments.”
To acquire detailed images of the fibres, which are only 12 microns across, the IR team modified the beamline for the experiment using a highly polished germanium crystal to focus the IR beam onto the fibres.
Lead author Srinivas Nunna received a post graduate research award from the Australian Institute of Nuclear Science and Engineering (AINSE) to support the study.
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Australians with cancer will be the first to benefit from the multi-million dollar Australian Cancer Research Foundation (ACRF) Detector launched at the Australian Synchrotron, fast-tracking cancer research by harnessing light a million times brighter than the sun.
Minister for Industry, Innovation and Science, Senator the Hon. Arthur Sinodinos, unveiled the ACRF Detector, which is akin to a turbocharged camera, and will take images at a speed and accuracy currently not possible at any other Australian research facility.
The detector will enable researchers, including those working in cancer, to more than double their outputs, gaining more answers at a faster rate.
Currently, more than 60 per cent of all the research conducted on the Synchrotron’s Micro Crystallography (MX2) beamline is dedicated to cancer research, helping scientists to understand and develop new drug targets and refine treatments for a disease that is the leading cause of death around the globe.
Top: Dr Tom Caradoc-Davies, Principal Scientist - MX beamline, explains the ACRF Detector to Australian Minister for Industry, Innovation and Science, Senator the Hon. Arthur Sinodinos with Lucy Jones and Professor Charlie Bond.
Bottom left: Professor Charlie Bond and Lucy Jones in discussion with Australian Synchrotron Director, Professor Andrew Peele.
Bottom right: Chairman of the ACRF Board, Tom Dery presents the cheque to ANSTO CEO, Dr Adi Paterson.
ACRF CEO, Professor Ian Brown, said ACRF and its supporters are proud to have provided the $2 million grant that facilitated the purchase of the ACRF Detector.
“The ACRF Detector is a vital, core piece of equipment for cancer and medical research in Australia, and one that will be used by cancer researchers from all institutes, hospitals and universities,” said Professor Brown.
“It shows the three-dimensional structure of proteins, which do most of the work in cells, identifying opportunities to neutralise those involved in cancer and promoting those that may protect us from cancer.”
The Synchrotron is operated by the Australian Nuclear Science and Technology Organisation. Australian Synchrotron Director, Professor Andrew Peele, said the leaps that will be enabled by the new detector will more than double the facility’s capacity to collect data, leading to more targeted and effective treatments and, ultimately, improved patient outcomes.
“This new capability will take a beamline that was previously at full capacity – booked for use at all available hours of the day – and find it an extra gear, so it can deliver more research, and arm researchers with clear representations of protein structures,” said Professor Peele.
“There are a lot of questions that still need to be answered in the world of cancer research, and by partnering with ACRF and speeding up the throughput of important research, we are bringing more solutions closer than ever before.
“We’re essentially shifting from dial-up internet to high-speed broadband, putting our foot on the accelerator of cancer research technology, providing faster protein analysis to turbocharge cancer research and facilitate significant discoveries.”
Senator Sinodinos said the new ACRF Detector is a great example of how collaboration between research facilities, not-for-profits and government can improve outcomes for the Australian community.
“This investment in Australian research and technology has the potential to increase and quicken the rate at which research turns into practical applications for patients and the community,” Senator Sinodinos said.
“High quality research, collaboration and smart investment are needed to ensure that new research and knowledge are supported, and I am thrilled to be here today to witness exactly that, and officially reveal the ACRF detector.”
Attending the launch of the ACRF Detector with Minister Sinodinos was researcher and protein crystallographer from the University of Western Australia, Professor Charlie Bond, who has utilised the MX2 beamline for extensive protein analysis, including research into the childhood cancer neuroblastoma.
They were also joined by Lucy Jones, who is focused on driving change in survival rates through increased research into neuroblastoma, having lost her daughter Sienna to the illness in 2010.
“Losing a child to neuroblastoma has driven me to do all I can to support research in finding an effective treatment for this insidious disease and other childhood cancers, made all the more challenging due to the high cost of drug development and the rarity of most childhood cancers,” Ms Jones said.
"We must do everything we can to help researchers such as Professor Bond, and innovative technologies such as this, to help make the whole research process more efficient by reducing costs and time to clearly benefit the research of childhood cancers and other diseases, shortening the time between lab discoveries and clinical testing of new drugs,” she said.
Neuroblastoma occurs most commonly in infants and children under five years of age. It is cancer made up of cells that are found in nerve tissues called neuroblasts, commonly found in adrenal glands and along tissues around the spinal cord in the neck, chest, abdomen and pelvis.
The ACRF Detector was made possible by a $2 million grant from the ACRF, and additional contributions from Monash University, CSIRO, La Trobe University, NZ Synchrotron Group, the University of Western Australia, the Walter and Eliza Hall Institute of Medical Research, the University of Melbourne, the University of Queensland, the University of Sydney, the University of Wollongong, Victor Chang Cardiac Research Institute, the University of Adelaide, Australian National University and ANSTO.
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Cross-Tasman collaboration between Australian and New Zealand researchers has shed light on a protein involved in diseases such as Parkinson’s disease, gastric cancer and melanoma.
Using the Australian Synchrotron, a team of researchers led by Dr Peter Mace from the University of Otago, in collaboration with Australian scientists investigated a protein called Apoptosis signal-regulating kinase 1 (ASK 1) with the results published today in leading international journal PNAS.
Dr Mace says the protein plays an important role in controlling how a cell responds to cell damage, and can push the cell towards a process of programmed cell death for the good of the body, if damage to a cell is too great.
“We now know a lot more about how ASK1 gets turned on and off – this is important because in diseases such as Parkinson’s, stomach cancer and melanoma, there can be either too much or too little ASK1 activity,” he said.
The ASK1 protein gets its name from an ancient Greek word meaning “falling off” – apoptosis – and is used to describe the process of programmed dying of cells – of the body actively killing them – rather than their loss by injury.
Researchers found that ASK1 has unexpected parts to its structure, that help control how the protein is turned on, and that an entire family of ASK kinases share these features.
Dr Mace says that the new findings add to our understanding of how cells can trigger specific responses to different threats or damage encountered, such as oxidants, which damage the body’s tissues by causing inflammation.
He adds that kinases are excellent targets for developing new drugs because they have a “pocket” in their structure that such compounds can bind to, but to develop better drugs we need to understand far more about how they are controlled. This is the goal of several projects in his lab, he says.
The research team determined ASK1’s molecular structure through crystallography studies – using the Synchrotron to see exactly what it is made up of – and performed other biochemical experiments to better understand the protein.
Dr Tom Caradoc-Davies, (below) Principal Scientist of the Macromolecular Crystallography and Micro Crystallography beamlines at the Australian Synchrotron, helped to collect data critical to the project.
Dr Tom Caradoc-Davies on the MX beamline at the Australian Synchrotron
“Using the Synchrotron’s MX Beamlines, we collected data from difficult samples, to help solve questions the research team had about the structure of the protein,” Dr Caradoc-Davies said.
“This is a great example of how regular access to the Synchrotron’s facilities can help move a project along more rapidly than otherwise would be the case, where it could take many years more for a team to find an answer, or they may not be able to find one at all.”
The study is a collaboration between Otago researchers and scientists at the Walter and Eliza Hall Institute (WEHI) in Melbourne, and at the Australian Synchrotron.
Access to this ANSTO landmark research infrastructure was enabled by the New Zealand Synchrotron Group, which is coordinated by the Royal Society of New Zealand and supported by all New Zealand universities in partnership with the Australian and New Zealand Governments.
The Australian Synchrotron is crucial to many other research projects from Otago and throughout New Zealand.
The study was supported by a Royal Society of New Zealand Rutherford Discovery Fellowship and grants from the University of Otago, the Victorian State Government and the National Health and Medical Research Council.