Finding the human ‘spring’ |
Thursday, 03 March 2011 | |
The University of Sydney An international team of scientists from Australia, the United Kingdom, the United States of America and Europe, led by the University of Sydney, has solved the structural puzzle of the main component of elastin. This protein gives our vital organs the ability to expand and contract. The discovery could lead to significant advances in treatment for burn victims and patients needing to replace damaged blood vessels. The findings, published in this month's edition of the highly acclaimed journal Proceedings of the National Academy of Sciences USA (PNAS), describe the spring-like structure of elastin's essential element, tropoelastin. Initiator and research project leader, Professor Tony Weiss from the School of Molecular Bioscience, said: "Tropoelastin is a tiny protein 'nano spring' in the human body. Our bodies assemble these nano springs to put elasticity into tissues such as skin, blood vessels and lungs." "Our finding results from more than a decade of international collaboration. Our scientific teamwork spans Australia, the UK, USA and Europe. We discovered that tropoelastin is a curved, spiral-shaped molecule with an attached 'foot' that helps it attach to human cells. "We also found that tropoelastin has the extraordinary capacity to extend to eight times its initial length and then return to its original shape with no energy loss, so it behaves like a perfect spring. Nature is showing us how to make an ideal nano spring." Professor Weiss said the discovery has significant implications for future treatment of skin repair such as in burns victims, and patients who need to replace damaged elastic blood vessels. "The elastin around our lungs, for example, expands with each intake of breath and contracts with each exhalation. Other vital organs such as our skin and arteries absolutely depend on it." Professor Weiss's co-author and international collaborator, Dr Clair Baldock from the Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, said: "Understanding how the structure of tropoelastin creates its exceptional elastic properties will hopefully enable the development of synthetic elastin-like polymers with potentially wide-ranging benefits." An international team of scientists from Australia, the United Kingdom, the United States of America and Europe, led by the University of Sydney, has solved the structural puzzle of the main component of elastin. This protein gives our vital organs the ability to expand and contract. The discovery could lead to major advances in treatment for burns victims and for patients who need to replace damaged blood vessels. The findings, published in this month's edition of the highly acclaimed journal Proceedings of the National Academy of Sciences USA (PNAS), describe the spring-like structure of elastin's essential element, tropoelastin. Initiator and research project leader, Professor Tony Weiss from the School of Molecular Bioscience, said: "Tropoelastin is a tiny protein 'nanospring' in the human body. Our bodies assemble these nanosprings to put elasticity into tissues such as skin, blood vessels and lungs." "Our finding is the result of more than a decade of international collaboration. Our scientific teamwork spans Australia, the UK, USA and Europe. We discovered that tropoelastin is a curved, spiral-shaped molecule with an attached 'foot' that helps it attach to human cells. "We also found that tropoelastin has the extraordinary capacity to extend to eight times its initial length and then return to its original shape, with no loss of energy, so it behaves like a perfect spring. Nature is showing us how to make an ideal nanospring." Professor Weiss said the discovery has significant implications for future treatment of skin repair such as in burns victims, and patients who need to replace damaged elastic blood vessels. "The elastin around our lungs, for example, expands with each intake of breath and contracts with each exhalation. Other vital organs such as our skin and arteries absolutely depend on it." Professor Weiss's co-author and international collaborator, Dr Clair Baldock from the Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, said: "Understanding how the structure of tropoelastin creates its exceptional elastic properties will hopefully enable the development of synthetic elastin-like polymers with potentially wide-ranging benefits." |
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