Structure–Property Relationships of Elastin-like Polypeptides: A Review of Experimental and Computational Studies

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 behavior, 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.

Lipidation Alters the Structure and Hydration of Myristoylated Intrinsically Disordered Proteins

“…Specifically, both computational and experimental studies indicate that the transition temperature of unmodified ELPs exhibits power-law dependence with length�i.e., (T t (GVGVP) n ∼ (n) −0.65 ). 70,71 Moreover, these results are not in agreement with trends based on the mean hydrophobicity approximation as determined by analytical HPLC.…”

Special Issue on Engineering Bioinspired and Biological Materials

“…Tropoelastin is the precursor protein which is watersoluble and forms a gel at physiological temperatures due to its lower critical solution temperature (LCST). Loṕez Barreiro et al 15 reviewed the structures and functions of elastin-like polypeptides (ELPs): recombinantly generated elastin-inspired biopolymers with motifs that mimic the repetitions of a tiny portion of the tropoelastin sequence. Importantly, ELPs have the same LCST and mechanical characteristics as tropoelastin, making them potential candidates for the creation of elastic and stimuli-responsive protein-based materials.…”

Exploring stimuli-responsive elastin-like polypeptide for biomedicine and beyond: potential application as programmable soft actuators

“…Since ELP is synthesized by recombinant DNA technology, it is feasible to develop fusion protein with other polypeptides and proteins to acquire synergistic properties. López Barreiro et al (2023) For example, silk fibroin is a natural protein mostly procured from silkworm increasingly used as scaffold material for biomedical applications. Similar to ELP, silk fibroin also contains characteristic peptide repeats (e.g., GAGAX, X: guest residue).…”