In the presence of water, elastin exists in the form of a rubbery extension with a low elastic modulus (Partridge, 1969). In addition, over 75% of the sequence of elastin consists of just four non-polar amino acids, namely, glycine, valine, alanine, and proline (Vrhovski and Weiss, 1998).

Stretched elastin isolated from bovine aorta. In the body, elastin is usually associated with other proteins in connective tissues. Elastic fiber in the body is a mixture of amorphous elastin and fibrous fibrillin. Both components are primarily made of smaller amino acids such as glycine, valine, alanine, and proline.

2022年3月4日 · The main amino acids that make up elastin are proline, glycine, desmosine and isodesmosine. They’re grouped in short, repeated sequences of three to nine amino acids which create strong, flexible structures.

Tropoelastin’s amino acid sequence predominantly consists of non-polar residues including glycine, valine, alanine, and proline (Debelle and Tamburro, 1999).

Elastin, or ELP is an important component in connective tissue which provides support and elasticity to tissues of the heart, lungs, skin, and blood vessels. The cross-linking in elastin occurs by two polyfunctional amino acids, i.e., desmosine and isodesmosine.

This finding, along with the ability of coacervate droplets to self-organize into extended network structures, suggests that the basic information needed for elastin assembly and elastomeric properties is provided by sequence motifs in the primary amino acid sequence of tropoelastin.

Further DNA sequencing should determine the complete amino acid sequence of elastin. Biosynthetic studies and in vitro translation of elastin mRNA have demonstrated that a 72,000-dalton polypeptide, designated tropoelastin, is the initial translation product.