Structure-property relationships of elastin-like polypeptides -- a review of experimental and computational studies
Diego L\'opez Barreiro, Inge J. Minten, Jens C. Thies, Cees M. J. Sagt

TL;DR
This review discusses how experimental and computational studies have advanced understanding of the relationship between structure and properties of elastin-like polypeptides, focusing on their LCST behavior and mechanical characteristics.
Contribution
It provides a comprehensive overview of recent experimental and computational insights into the structure-property relationships of ELPs, aiding future material design.
Findings
ELPs exhibit LCST and mechanical properties similar to tropoelastin.
Sequence variations influence ELP phase transition and elasticity.
Computational models help predict ELP behavior based on sequence.
Abstract
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…
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