Human islet amyloid polypeptide oligomers stabilized and probed by MAS NMR

作     者：Ziwei Chang Zhengfeng Zhang Ziwei Chang;Zhengfeng Zhang

作者机构：Key Laboratory of Magnetic Resonance in Biological SystemsState Key Laboratory of Magnetic Resonance and Atomic and Molecular PhysicsNational Center for Magnetic Resonance in WuhanInnovation Academy for Precision Measurement Science and TechnologyChinese Academy of SciencesWuhan430071China 

出 版 物：《Magnetic Resonance Letters》 (磁共振快报（英文）)

年 卷 期：2024年第4卷第1期

页      面：61-62页

学科分类：081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 070305[理学-高分子化学与物理] 080501[工学-材料物理与化学] 0805[工学-材料科学与工程（可授工学、理学学位）] 0703[理学-化学] 0702[理学-物理学] 

主　　题：aggregation oligomer stabilized 

摘      要：The capture and characterization of oligomers are extremely important in the studies of amyloid aggregation of proteins and *** are critical intermediates that can impact the structures of amyloid ***,it is widely accepted that oligomers are the most toxic species along the aggregation pathway[1e4].The studies of oligomers are believed to shed light on the molecular mechanism of amyloid fibrillation and probably the medical clues for related *** vitro investigations of amyloid oligomers are challenging due to their transient and polymorphic nature[5].This is particularly evident in the case of human type-2 diabetes-associated islet amyloid polypeptide(hIAPP),which tends to rapidly form polymorphic fibrils within minutes[6].Notably,hIAPP demonstrates a higher propensity for rapid aggregation compared to other amyloid proteins such as a-synuclein[7].