Elastin biological properties

In Nature, there are many examples of protein and peptide molecular self-assembly. Of the genetically engineered fibrous proteins, collagen, spider silks, and elastin have received attention due to their mechanical and biological properties which can be used for biomaterials and tissue engineering. 

The synthesis of well-defined macromolecular structures with controlled properties is critical for the production of advanced materials for biological and industrial applications. Inspired by nature s ability to create proteins with exquisite control, we focus on the applications of elastin and elastin-derived polymers for materials design. The elucidation of elastin biochemical, conformational and physical properties offers insight into the fabrication of novel biomaterials. As part of this review, we highlight some of the recent advances that permit the generation of customized elastin-based polymers. These developments provide an added level of control vital to the future construction of tailor-made supramolecular structures with emergent physical, mechanical and biological properties. 

A particular kind of materials are the silk-elastin-like protein polymers (SELPs), consisting of the repeating units of silk and elastin blocks, which combine a set of outstanding physical and biological properties of silk and elastin. SELPs can undergo tunable... 

This chapter will discuss the basic aspects of elastin and resilin and will address their biological role, biochemical processing, and properties. The materials inspired by elastin and resilin, such as elastin-like polypeptides and resilin-like polypeptides, and applications thereof, will also be covered. 

The advantage of an entropic mechanism of elastomeric force is that it depends on the decrease in the number of accessible states on extension and can be considered ideal for a biological elastomer that is required to be durable, such as elastin. In contrast, the elastomeric properties of the HMW subunits and other gluten proteins... 

The work on metabolic turnover underlines the biological and chemical unreactivity of elastin which is perhaps its most characteristic property. Apart from the destructive effects of recognizable disease it has seemed to many authors that the mature elastic fiber, once laid down, is retained for life. In this situation it may be expected that changes may occur in elastic fibers which could be ascribed to the results of aging alone. Such changes have been looked for in a number of laboratories. 

The precise understanding of the structural nature of elastin remains elusive because the unusual physical properties of native elastin have prevented the use of traditional structural biology techniques. The hydrophobic domains are dominated by a pentapeptide repeat sequence of (Val-Pro-Gly-Val-Gly). This repeat sequence is believed to endow elastin its remarkable elastic properties, allowing continual expansion and contractions without loss of structural integrity (2). 

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