Elastin structural properties

Structural proteins are commonly fibrous proteins such as keratin, collagen and elastin. Skin, bone, hair and silk all depend on such proteins for their structural properties. 

The first elastomeric protein is elastin, this structural protein is one of the main components of the extracellular matrix, which provides stmctural integrity to the tissues and organs of the body. This highly crosslinked and therefore insoluble protein is the essential element of elastic fibers, which induce elasticity to tissue of lung, skin, and arteries. In these fibers, elastin forms the internal core, which is interspersed with microfibrils [1,2]. Not only this biopolymer but also its precursor material, tropoelastin, have inspired materials scientists for many years. The most interesting characteristic of the precursor is its ability to self-assemble under physiological conditions, thereby demonstrating a lower critical solution temperature (LCST) behavior. This specific property has led to the development of a new class of synthetic polypeptides that mimic elastin in its composition and are therefore also known as elastin-like polypeptides (ELPs). 

Resilin and elastin, unlike other structural proteins, fulfill both definitions of an elastic material. Colloquially speaking, resilin and elastin are stretchy or flexible. They also fulfill the strict definition of an elastic material, i.e., the ability to deform in proportion to the magnitude of an applied stress without a loss of energy, and the recovery of the material to its original state when that stress is removed. Resilin and elastin are alone in the category of structural proteins (e.g., collagen, silk, etc.) in that they have the correct blend of physical properties that allow the proteins to fulfill both definitions of elasticity. Both proteins have high extensibility and combine that property with remarkable resilience [208]. 

Elastin is a structural protein with outstanding properties, and therefore it has inspired many investigations, with special interest in its elastomeric properties. This behavior can be mimicked with ELPs and these have found wide application in... 

The pleural tissue is a typical connective tissue that consists mostly of matrix the fibrous proteins (collagen, elastin), and mucopolysaccharides, and a few scattered mesothelial cells, capillaries, venules, and ducts. Anatomists have defined several layers (Fig. 3.4) for each of the pleura. Layers 3 and 5 in Fig. 3.4 contain an abundance of fibrous protein, especially elastin. Both the interstitial (Layer 4) and mesothelial (1 and 2) layers contain capillaries of the vascular system and lymphatic channels. The matrix (ground substance) gives the pleura structural integrity and is responsible for its mechanical properties such as elasticity and distensibility. 

Native elastin is an insoluble, highly cross-linked protein. The chemistry, properties and structure of elastin have been frequently reviewed in the past330-333. In this context, aspects of calcification processes will be discussed. 

Collagen and elastin are examples of common, well-characterized fibrous proteins that serve structural functions in the body. For example, collagen and elastin are found as components of skin, connective tissue, blood vessel walls, and sclera and cornea of the eye. Each fibrous protein exhibits special mechanical properties, resulting from its unique structure, which are obtained by combining specific amino acids into reg ular, secondary structural elements. This is in contrast to globular proteins, whose shapes are the result of complex interactions between secondary, tertiary, and, sometimes, quaternary structural elements. 

The fundamental driving force behind the remarkable elastic properties of the elastin polymer is believed to be entropic, where stretching decreases the entropy of the system and elastic recoil is driven by a spontaneous return to maximum entropy. The precise molecular basis for elasticity has not been fully elucidated and a number of models exist. Two main categories of structure-function models have been proposed those in which elastin is considered to be isotropic and devoid of structure, and those which consider elastin to be anisotropic with regions of order (Vrhovski and Weiss, 1998). 

Despite different sequences and repetitive motives, all gliadins have the same secondary structure of loose spirals which are a balanced compromise between the p-spiral and poly-L-proline structure (polyproline helix II) (Parrot et al., 2002), the balance is dependent on temperature, type of solvent, and hydration level (Miles et al., 1991). Similar sequences can be found in other proteins, mainly animal proteins such as elastin and collagen, and they are responsible for particular biomechanical properties connected to reverse P-spirals or p-sheet structures (Tatham and Shewry, 2000). 

The protein elastin presents another opportunity to create amyloid-like fibrils from natural proteins for the purpose of developing biomaterials. Elastin is found in tissue where it imparts elastic recoil, and fibrils formed from this protein may demonstrate some of the elastic properties of the constituent elastic proteins (Bochicchio et al., 2007). Elastin typically contains the sequence poly(ZaaGlyGlyYaaGly) (where Zaa, Yaa = Val or Leu) (Tamburro et al., 2005), and short stretches of the protein retain the ability to form structures similar to the original protein. Simple proline to glycine mutations in the hydrophobic domains of elastin can induce the formation of amyloid-like fibrils (Miao et al., 2003), suggesting that fibrillar materials can be easily generated from these sequences. 

The four protein conformations that provide mechanical stability to cells, tissues, and organs include the random coil or amorphous structure that characterizes a part of the structure of elastin, the a helix, which is represented by the keratin molecule, the collagen triple helix, and the p structure of silk. In humans the P structure is found only in short sequences connecting parts of other structures such as the a helix, but serves as an example of the relationship between protein structure and properties. The ultimate tensile strength and modulus of each structure differs as discussed below. 

Our last example of the mechanical properties of a protein is that of keratin found in the top layer of skin. The stratum corneum in skin is almost exclusively made up of different keratins that have an a-helical structure. The helices do not run continuously along the molecule so the structure is not ideal. However, the stress-strain characteristics are shown in Figure 6.4 and demonstrate that at low moisture content the stress-strain curve for keratins in skin is approximately linear with a UTS of about 1.8 GPa and a modulus of about 120 MPa. These values are between the values reported for elastin and silk, which is consistent with the axial rise per amino acid being 0.15 nm for the a helix. Thus the a helix with an intermediate value of the axial rise per amino acid residue has an intermediate value of the... 

We now well appreciate, of course, that polymers are virtually everywhere. Some of them occur naturally, and we continue to better understand their compositions, structures, and properties. Many of these materials have been used since the dawn of human existence, for food, obviously. Cellulose alone has been essential for clothing, fire, shelter, tools, weapons, writing, and art. Leather is probably the result of the first synthetic polymer reaction, essentially the crosslinking of protein (elastin). How we progressed over time to the Polymer Age is a fascinating series of stories, some of which are well worth recounting here. 

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