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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.
摘要：
弹性蛋白是一种具有出色机械性能的结构蛋白(例如，弹性和弹性)和生物学相关功能(例如，触发反应，如细胞粘附或趋化性)。它由其前体原弹性蛋白形成，一种在生理温度下凝聚的60-72kDa水溶性和温度响应蛋白，经历一种称为低临界溶液温度(LCST)的现象。受到这种行为的启发，许多科学家和工程师正在开发重组生产的弹性蛋白生物聚合物，通常称为弹性蛋白样多肽(ELPs)。这些ELP通常由具有序列VPGXG的重复基序组成，对应于小部分原弹性蛋白序列的重复，X是除脯氨酸以外的任何氨基酸。ELPs表现出与原弹性蛋白相似的LCST和机械性能，这使它们成为开发弹性和刺激响应性蛋白质材料的有希望的候选人。通过建立ELP氨基酸序列与材料宏观性质之间的联系，揭示ELP的结构-性质关系可以帮助这些材料的开发。在这里，我们对ELP和ELP基材料的结构-性能关系进行了综述，重点关注LCST和机械性能以及实验和计算研究如何帮助他们理解。
