Elastin is a vital component of flexible tissues, and poorly maintained in the adult body. Deterioration of elastin is an important component of the age-related structural alterations that take place in tissues such as skin and blood vessels. Elastin is also hard to obtain or manufacture for use in engineered tissues, which is the primary roadblock motivating the research noted here. While this is useful, a robust source of elastin (or as here, elastin-like proteins that suitably mimic the behavior of elastin) would probably do relatively little to enable therapies to restore elastin structures in aged tissues, as those elastin structures are complex and the configuration of elastin molecules relative to other components of the extracellular matrix matters. It is likely that some form of reprogramming of cell behavior will be necessary to rebuild the elastin structures that were primarily laid down during development.
Our bodies contain a special protein called elastin, which has a remarkable ability to stretch like a rubber band and snap back to its original shape. This elasticity is crucial for the function of various organs, allowing the lungs to inhale and exhale, blood vessels to expand and contract with each heartbeat, and the skin to remain smooth and supple. Despite its utility, using natural elastin for medical applications is challenging. It’s available in limited quantities naturally, the purification process is complex, and there’s a risk of an immune reaction when administered to humans in other individuals. To address these issues, scientists developed elastin-like polypeptides (ELPs), which could be produced in large quantities but could not fully replicate the complex, precise functions of natural elastin.
Researchers have now created a new protein by selecting and reassembling the most critical parts of tropoelastin, the precursor to human elastin. They precisely combined three distinct domains – a hydrophobic domain that influences the protein’s physical properties, a cross-linking domain that provides stability, and a cell-interaction domain that promotes interactions between cells. This new protein was named elastin domain-derived protein (EDDP). EDDP offers several advantages. It can be mass-produced like conventional ELPs while retaining the elasticity and resilience comparable to natural elastin. More remarkably, EDDP promotes cell adhesion and growth by transmitting signals that were lacking in conventional ELPs. This enhanced cell-interaction function directly aids cell survival and growth, making it highly effective in regenerating damaged tissues.
Link: https://www.postech.ac.kr/eng/research/research_results.do?mode=view&articleNo=35356
