Chemical Biology Laboratory, National Cancer Institute, National Institutes of Health, Frederick, MD, 21702, United States.
Chemical Biology Laboratory, National Cancer Institute, National Institutes of Health, Frederick, MD, 21702, United States.
Curr Opin Chem Biol. 2021 Oct;64:131-144. doi: 10.1016/j.cbpa.2021.06.006. Epub 2021 Jul 29.
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.
20 多年来，肽材料以水凝胶或可溶性纤维的形式一直被用于生物医学应用，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转化，仍需要解决关键的研究领域。与淀粉样蛋白相比，它们的结构特征还不够完善。许多旨在指导材料形成的结构特征主要是通过观察淀粉样蛋白组装体的原子分辨率结构来进行表征的。在此，本文将探讨这些基序与肽设计的关系，确定共同的相互作用，这些相互作用驱动组装并提供结构特异性。这里综述的设计复杂结构的当前努力突出表明，需要将淀粉样蛋白的结构革命扩展到肽组装体，以验证设计原则。就临床应用而言，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未得到很好的理解。只有少数趋势现在才刚刚开始出现肽材料与生物系统的相互作用。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。
