Genetically engineered proteins
represent a new promising class of biomaterials that
overcome the disadvantages of naturally derived
biopolymers (potential pathogens transmission, immune
reactions, etc). These engineered macromolecules contain
repeated natural sequence motifs that induce a regular
structure and self-assembly capability. Many recent
examples show the potentiality of application of elastinlike
polypeptides (ELP) for a wide range of biomedical
applications that exploit their features.
This work aims at designing and producing, by
recombinant DNA methodology, a human elastin-like
artificial protein (HELP) as starting material for the
preparation of self-assembled or crosslinked matrices to
be used in regenerative medicine. On the basis of the
VAPGVG sequence (the most structurally regular
occurring region of the human tropoelastin) a synthetic
gene was designed, cloned and expressed in Escherichia
coli. The obtained artificial HELP protein (an eight
block protein polymer, MW » 45000 Da) includes
substrate amino acids (K, lysine and Q, glutamine) for
enzymatic crosslinking.