Department of Chemistry, University of South Florida, 4202 E. Fowler Avenue, Tampa, FL, 33620, USA.
Angew Chem Int Ed Engl. 2018 Jul 26;57(31):9916-9920. doi: 10.1002/anie.201805184. Epub 2018 Jul 3.
The development of peptidomimetic helical foldamers with a wide repertoire of functions is of significant interest. Herein, we report the X-ray crystal structures of a series of homogeneous l-sulfono-γ-AA foldamers and elucidate their folding conformation at the atomic level. Single-crystal X-ray crystallography revealed that this class of oligomers fold into unprecedented dragon-boat-shaped and unexpected left-handed helices, which are stabilized by the 14-hydrogen-bonding pattern present in all sequences. These l-sulfono-γ-AApeptides have a helical pitch of 5.1 Å and exactly four side chains per turn, and the side chains lie perfectly on top of each other along the helical axis. 2D NMR spectroscopy, computational simulations, and CD studies support the folding conformation in solution. Our results provide a structural basis at the atomic level for the design of novel biomimetics with a precise arrangement of functional groups in three dimensions.
具有广泛功能的拟肽螺旋折叠物的发展具有重要意义。本文报道了一系列均一的 l-磺酸基-γ-AA 折叠物的 X 射线晶体结构，并在原子水平上阐明了它们的折叠构象。单晶 X 射线晶体学揭示，这类低聚物折叠成前所未有的龙舟形和出乎意料的左手螺旋，所有序列中存在的 14 氢键模式稳定了这些螺旋。这些 l-磺酸基-γ-AA 肽具有 5.1Å 的螺旋螺距和每圈恰好四个侧链，侧链沿螺旋轴完美地彼此堆叠。2D NMR 光谱、计算模拟和 CD 研究支持溶液中的折叠构象。我们的结果为设计具有精确三维功能基团排列的新型仿生物提供了原子水平的结构基础。
