Elastin’s Remarkable Flexibility Explained

Research Updates
Scientists have unlocked the secret of elastin’s spectacular flexibility in a discovery that helps Australian scientists engineer even better synthetic replacement blood vessels.

The Heart Research Institute in Sydney has been involved in a major international study that delves into the movement of elastin, a crucial building block which makes our organs and blood vessels flexible.

The research, led by Professor Anthony Weiss at University of Sydney and by collaborators at MIT, investigates the hierarchical structure of scissor-shaped molecules that gives elastin its remarkable properties.

"Through a combination of computer modelling and lab work, we were able to reveal for the first time the shape, structure and true nature of the basic tropoelastin molecule, the protein that makes up elastin tissues,” explains HRI’s Dr Steven Wise, a contributor to the study published in the journal Science Advances.

“This knowledge could explain why some diseases weaken blood vessels and will also help us artificially engineer better life-saving new tissue to use in patients.”

Elastin is a highly elastic protein that is a critical component of all the elastic organs of the body, including skin, heart, lungs, bladder, veins and large arteries. 

“Thanks to elastin, our skin can stretch and twist, our blood vessels can expand and relax and lungs can swell and contract, but until now we haven’t really understood this incredible flexibility,” Dr Wise says.

“It’s great to continue working with the study’s lead author Giselle Yeo and Professor Weiss, as I did my PhD studies in that lab, investigating tropoelastin.” 


The study used a type of particle accelerator called a synchrotron - which propels charged particles to near light speed - to gather information about the structural and chemical properties of tropoelastin molecules.

Researchers discovered that the scissor-shaped bump of one tropoelastin molecule connects to the narrow part of another, eventually building up a chain.

As he explains, the research team now have a far more complex understanding of the molecule. “It looks almost like a ballerina doing a graceful dance, opening and closing its legs repeatedly until the ballerinas sit in a long line, with one piggybacking on the next,” the scientist says. “These chains build up to create the extraordinarily flexible tissue the human body relies on to make our organs, thereby creating life.”

The findings explain a lot about the molecule’s natural flexibility, and could prove useful medically, to explain why blood vessels become weakened in people with certain disease conditions.

For the HRI however, it’s the potential for this information to help build better synthetic blood vessel replacements that has researchers excited.

“We use elastin in our stent program and in our synthetic blood vessel engineering, so the study helps us better understand the building blocks used in that work,” Dr Wise says.

“Ultimately we’d like to apply this research to medical practice and we continue working closely with Professor Weiss’s team to work toward this goal.”

The research team, which also included the University of Manchester in the United Kingdom, was supported by grants from the Australian Research Council, the National Institutes of Health, the BBSRC, Wellcome Trust and the Office of Naval Research.


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