Molecular Underpinning of Flexible Elastin Tissue Unveiled - European Medical Journal

Molecular Underpinning of Flexible Elastin Tissue Unveiled

1 Mins

MYSTERIOUS mechanisms of elastin tissue, a vital aspect of enabling our body to function, have finally been revealed through a novel combination of techniques in a recent study by an international team of collaborators.

The protein-based tissue is responsible for creating flexibility in the body; it enables the most rudimentary functions such as movement, the heartbeat, and breathing. Counter-intuitive though it may seem, this basic characteristic is governed by the intricately complex molecular structure of the protein tropoelastin. This protein is also incredibly resistant, surviving a human lifespan and experiencing up to two billion cycles of blood vessel pulsation.

The scientific agenda has long prioritised investigation of elastin, and this study has demonstrated a multidisciplinary approach revealing the significance of the helical structure to the protein’s flexibility. “It’s almost like a dance the molecule does, with a scissors twist – like a ballerina doing a dance” said Prof Anthony Weiss, McCaughey Chair in Biochemistry, Charles Perkins Centre, University of Sydney, Sydney, Australia. To understand the natural flexibility, the researchers rendered genetically modified elastin proteins for comparison. Modelling the movements of each molecule, the researchers found that both overall shape and regional structure were at play. The scissor-like facet of one molecule naturally latches onto the narrow end of another in a continuous lock and key pattern.

Investigating the complexity of this process required a 3-fold approach of considerable finesse, atomic-scale computational modelling of the molecular structure, synchrotron imaging of its three-dimensional form, and modified genetic comparison. This combination enabled the study of elastin at both a sub-molecular and single-molecule scale, illuminating the mechanisms behind its dynamic properties. Using this technique to compare genetically nuanced elastin proteins yielded dramatic results, and suggests that even a slight mutation may explain weakened blood vessels in certain diseases.

The study also has some exciting avenues of application beyond elastin. “We are excited about the new opportunities that arise from this collaboration and the potential for future work, because designing materials that last for many decades without breaking down is a major engineering challenge that nature has beautifully accomplished, and on which we hope to build,” commented Prof Markus Buehler, Department Head, Faculty of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.


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