Elastinähnliche

Elastinähnliche, often abbreviated as ELP, refers to a class of intrinsically disordered proteins that mimic the biophysical properties of elastin, a major component of elastic tissues in vertebrates. Unlike fibrous proteins like collagen, elastin is a highly flexible and resilient protein that allows tissues to stretch and recoil. ELPs are designed polypeptides that recapitulate this elasticity.

These engineered proteins are typically synthesized using a repeating sequence of amino acids, often derived from the natural sequence of elastin, which includes a high proportion of glycine, valine, proline, and alanine. The specific sequence and length of these repeats can be tailored to achieve desired mechanical properties. A key characteristic of ELPs is their inverse temperature transition behavior. Below a certain temperature, they are soluble in aqueous solutions. However, upon heating above this transition temperature, they aggregate and can form hydrogels or films. This phase transition is driven by a decrease in hydrophobic interactions as the temperature increases, leading to the expulsion of water and protein-protein association.

The tunable nature of ELPs, from their mechanical elasticity to their phase transition behavior, makes them attractive for a wide range of applications. They are being explored in biomaterials for tissue engineering, drug delivery systems, and as components in biosensors. Their biocompatibility and ability to self-assemble into various structures further enhance their potential in these fields. Researchers continue to modify ELP sequences to fine-tune their properties for specific biomedical and industrial uses.