Institute of Chemistry, University of Manitoba, Dysart Rd. 144, R3T 2N2, Winnipeg, Manitoba, Canada.
Org Biomol Chem. 2019 Sep 21;17(35):8031-8047. doi: 10.1039/c9ob01646e. Epub 2019 Aug 29.
Collagen mimics are peptides designed to reproduce structural features of natural collagen. A triple helix is the first element in the hierarchy of collagen folding. It is an assembly of three parallel peptide chains stabilized by packing and interchain hydrogen bonds. In this review we summarize the existing chemical approaches towards stabilization of this structure including the most recent developments. Currently proposed methods include manipulation of the amino acid composition, application of unnatural amino acid analogues, stimuli-responsive modifications, chain tethering approaches, peptide amphiphiles, modifications that target interchain interactions and more. This ability to manipulate the triple helix as a supramolecular self-assembly contributes to our understanding of the collagen folding. It also provides essential information needed to design collagen-based biomaterials of the future.
胶原模拟物是设计用来复制天然胶原结构特征的肽。三螺旋是胶原折叠层次结构中的第一个要素。它是由三个平行的肽链组装而成，通过包装和链间氢键稳定。在这篇综述中，我们总结了现有的稳定这种结构的化学方法，包括最新的进展。目前提出的方法包括操纵氨基酸组成、应用非天然氨基酸类似物、响应性修饰、链连接方法、肽两亲体、针对链间相互作用的修饰等。这种操纵三螺旋作为超分子自组装的能力有助于我们理解胶原折叠。它还提供了设计未来基于胶原的生物材料所需的重要信息。
