For over 20 years, peptide materials in their hydrogel or soluble fibril form have been used for biomedical applications such as drug delivery, cell culture, vaccines, and tissue regeneration. To facilitate the translation of these materials, key areas of research still need to be addressed. Their structural characterization lags compared to amyloid proteins. Many of the structural features designed to guide materials formation are primarily being characterized by their observation in atomic resolution structures of amyloid assemblies. Herein, these motifs are examined in relation to peptide designs identifying common interactions that drive assembly and provide structural specificity. Current efforts to design complex structures, as reviewed here, highlight the need to extend the structural revolution of amyloid proteins to peptide assemblies to validate design principles. With respect to clinical applications, the fundamental interactions and responses of proteins, cells, and the immune system to peptide materials are still not well understood. Only a few trends are just now emerging for peptide materials interactions with biological systems. Understanding how peptide material properties influence these interactions will enable the translation of materials towards current and emerging applications.

中文翻译：

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从结构到应用：肽材料发展的进展与机遇。

20 多年来，水凝胶或可溶性原纤维形式的肽材料已用于生物医学应用，例如药物输送、细胞培养、疫苗和组织再生。为了促进这些材料的翻译，仍然需要解决关键的研究领域。与淀粉样蛋白相比，它们的结构特征滞后。许多旨在引导材料形成的结构特征主要是通过在淀粉样蛋白组装体的原子分辨率结构中观察到的来表征的。在此，检查这些基序与肽设计的关系，确定驱动组装并提供结构特异性的常见相互作用。正如本文所述，当前设计复杂结构的努力强调需要将淀粉样蛋白的结构革命扩展到肽组装以验证设计原理。在临床应用方面，蛋白质、细胞和免疫系统对肽材料的基本相互作用和反应仍不清楚。肽材料与生物系统的相互作用目前仅出现一些趋势。了解肽材料特性如何影响这些相互作用将使材料能够转化为当前和新兴的应用。