Looking at the way protein clusters form in long-life milk is allowing scientists to better understand Alzheimer's, Parkinson's and other age-related conditions.
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Co-lead researcher Professor John Carver of the ANU said there was no evidence ultra-high temperature (UHT) milk could cause these age-related conditions.
However, the unassuming pantry item was opening the door to better understanding how proteins clumped and clustered in conditions such as type 2 Diabetes, Alzheimer's, Parkinson's which affect more than 500 million people worldwide.
Professor Carver said milk proteins changed structurally when they were heated briefly to around 140 degrees to produce UHT milk, causing a gelling phenomenon with long-term storage.
The protein clusters which caused UHT milk to transform into a liquid gel were the same kind of toxic protein cluster found in plaque deposits in the brains of Alzheimer's and Parkinson's patients.
"Understanding the structures that are formed in the two milk proteins is directly analogous to what occurs in these diseases," Professor Carver said.
"Understanding the process of amyloid fibril formation will help us potentially in understanding what causes these diseases and treatments to prevent the aggregation from occurring."
The ANU research was conducted in partnership with CSIRO and the University of Wollongong and published in the journal Small.
Professor Carver has been studying milk proteins for more than a decade and said the findings of the study were crucial to curbing the onset of diseases that impacted Australia's ageing population.
"There are now over 50 different disease that have been recognised as being associated with protein aggregation," he said. "The vast majority of those diseases are age-related."
The diseases are associated with the body's chemistry slowing down and not being as efficient in getting rid of these toxic amyloid fibril protein aggregations.
To stem the development of the diseases through treatments, scientists need to expand their understanding of how our bodies regulate protein levels, and what prevents and destroys protein aggregation in the body.
"It will basically cripple our health care budget in the next 20 to 30 years if we don't come up with some means of preventing or at least staving off the development of these types of diseases."
"Any means we can understand these proteins, their structure and why they form amyloid fibrils has the potential for developing treatments."
