Wang Yishen, Yin Haizhi, Yang Yanling, Li Zheng-Hui, Li Gao-Wei, Lei Xinxiang
School of Pharmaceutical Sciences, South-Central Minzu University, Wuhan, 430074, China.
College of Chemistry and Chemical Engineering, Shangqiu Normal University, Shangqiu, 476000, China.
Magn Reson Lett. 2024 Dec 4;5(2):200171. doi: 10.1016/j.mrl.2024.200171. eCollection 2025 May.
The multiple oligopeptides have been regarded as promising alignment media due to their structural diverseness and tendency for self-assembly in solution. Herein, an assembled amphiphilic peptide alignment medium, i.e., C-CONH-Phg-Phg-IIIKK-CONH with unnatural amino acids for the determination of anisotropic parameters of NMR is introduced. The amphiphilic peptide can be self-assembled at low concentrations in DMSO and is stable and highly homogeneous. The NMR spectrum collected with the addition of the medium had fewer background signals. The utility of the acquired RDC data is demonstrated to determine relative configuration of three natural products, Helminthosporic acid, Estrone, and α-Santonin.
由于其结构多样性和在溶液中自组装的倾向，多种寡肽被认为是很有前景的排列介质。在此，引入了一种组装的两亲性肽排列介质，即用于核磁共振各向异性参数测定的含有非天然氨基酸的C-CONH-Phg-Phg-IIIKK-CONH。这种两亲性肽在二甲基亚砜中低浓度时即可自组装，且稳定且高度均匀。添加该介质后收集的核磁共振谱背景信号较少。所获得的剩余偶极耦合（RDC）数据用于确定三种天然产物——蠕孢酸、雌酮和α-山道年的相对构型。
