Human islet amyloid polypeptide oligomers stabilized and probed by MAS NMR  

作　　者：Ziwei Chang Zhengfeng Zhang 

机构地区：[1]Key Laboratory of Magnetic Resonance in Biological Systems,State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics,National Center for Magnetic Resonance in Wuhan,Innovation Academy for Precision Measurement Science and Technology,Chinese Academy of Sciences,Wuhan,430071,China

出　　处：《Magnetic Resonance Letters》2024年第1期61-62,共2页磁共振快报（英文）

摘　　要：The capture and characterization of oligomers are extremely important in the studies of amyloid aggregation of proteins and peptides.Oligomers are critical intermediates that can impact the structures of amyloid fibrils.Moreover,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 diseases.In 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].

关 键 词：AGGREGATION OLIGOMER STABILIZED 

分 类 号：R446[医药卫生—诊断学]