Researchers have decoded the molecule that gives flexibility to living tissue

The tendency of living tissues to expand, compress, stretch and bend over their lifetime is the result of a protein molecule called tropiolastin. It should be noted that this molecule can stretch up to eight times and return to its original size again.

Now, for the first time, researchers have decoded the molecular structure of this complex molecule, as well as the details of what can go wrong with its structure in various genetically induced diseases.

Troproplastine is the precursor molecule of elastin, which with the structures called microfibrils is the key to tissue flexibility, including skin, lungs and blood vessels. But the molecule is complex, made up of 698 amino acids and is full of disturbed areas.

This challenge was solved by a group of researchers who used a combination of molecular modeling and experimental observation to create an image of a person (per person) for the structure of the molecule. The results were published this week by Markus Buehler, Jerry McAfee and Anna Tarakanova in the Proceedings of the National Academy of Sciences. All this work has been done in collaboration with three universities: the MIT, the Massachusetts Institute of Technology, the University of Sydney and the University of Manchester.

The study showed that some different pathogenic mutations in the single gene that controls the formation of tropioplastin alter the stiffness and dynamic responses of the molecule, which could eventually help design treatments or countermeasures for these conditions . Other "artificial" mutations induced by the researchers, which do not correspond to any known natural mutation, can be used to better understand the function of the particular part of the gene affected by this mutation.