  Elastin is a structural protein with outstanding mechanical properties (e.g.,
elasticity and resilience) and biologically relevant functions (e.g.,
triggering responses like cell adhesion or chemotaxis). It is formed from its
precursor tropoelastin, a 60-72 kDa water-soluble and temperature-responsive
protein that coacervates at physiological temperature, undergoing a phenomenon
termed lower critical solution temperature (LCST). Inspired by this behaviour,
many scientists and engineers are developing recombinantly produced
elastin-inspired biopolymers, usually termed elastin-like polypeptides (ELPs).
These ELPs are generally comprised of repetitive motifs with the sequence
VPGXG, which corresponds to repeats of a small part of the tropoelastin
sequence, X being any amino acid except proline. ELPs display LCST and
mechanical properties similar to tropoelastin, which renders them promising
candidates for the development of elastic and stimuli-responsive protein-based
materials. Unveiling the structure-property relationships of ELPs can aid in
the development of these materials by establishing the connections between the
ELP amino acid sequence and the macroscopic properties of the materials. Here
we present a review of the structure-property relationships of ELPs and
ELP-based materials, with a focus on LCST and mechanical properties and how
experimental and computational studies have aided in their understanding.
