New insights are being discovered about elastic assembly, with research efforts focusing on how body tissue is able to stretch or shrink for various functions. Elastic fibers play a pivotal role in maintaining the extracellular matrix, the ECM network that consists of collagen, enzymes, proteins, and other minerals that provide cellular support. Within the extracellular matrix, elastin functions as a protein that provides elastic connective tissue, allowing our bodies greater flexibility and range of motion. Elastin is made up of other components such as tropoelastin – and studying tropoelastin will give us a better idea of how to potentially improve the elastic assembly.

A Deeper Understanding of Fibers, Elastins, and Tropoelastins

Elastic fibers are found in the tissue of the skin, lungs, cardiovascular organs, cartilage, and tendons. The fibers allow for improved biomechanical resilience, durability, and cell interactivity. About 90% of the elastic fibers are made up of elastin, while the remaining components are made up of fibrillin glycoproteins. The properties that make up these fibers are able to stretch and recoil in cycles – while also maintaining the structure of the tissues over the organism’s lifespan. The production of elastin primarily happens during prenatal and childhood development, but its synthesis tends to slow down during adulthood.

Tropoelastin acts as a precursor to elastin; it’s a soluble protein that’s being studied for its elastic properties. This protein has a spring-like molecular structure that can stretch up to eight times its resting length. Tropoelastin doesn’t express a lot of energy loss during its extension, keeping its structure in place. Both tropoelastin and elastin work toward forming biomaterials used for tissue engineering and regenerative medicine.

Tropoelastin in Gene Expressions, Sequences, and Elastogenesis

Tropoelastin is encoded by the ELN gene, the set of instructions that produces certain proteins. In recent years, studies have been examining the variations of spliced ELN mRNA transcriptions, looking into the diversity of these genes and how they could potentially be fine-tuned for better tissue function. Recent research has been testing how domain insertions and deletions tend to change the functionality of tropoelastin.

Computational modeling has helped to develop this area of study, with methodologies being used to closely examine the scale of the molecular structures. Using this modeling, researchers have proposed that the flexibility of mid-range molecules is what drives the overall elasticity of these fibers, with the flexible hinge regions between domains 21 and 23 showing scissors-like bending that contributes to the assembly.

Conclusion on Tropoelastin Research

Tropoeplastin is a unique protein that allows the self-assembly of elastic fibers to occur. Because tropoelastin’s sequence and structures are in a delicate balance, changes to the sequences could have far-reaching consequences. Some are predicting that cryogenic electron microscopy will be used to study flexible molecules. As the computational modeling and the research for this field develops, so will our understanding of tropoelastins and elastic assembly.