大鼠胰岛淀粉样多肽的膜结合反平行二聚体。
A membrane-bound antiparallel dimer of rat islet amyloid polypeptide.
机构信息
Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520-8114, USA.
出版信息
Angew Chem Int Ed Engl. 2011 Nov 11;50(46):10859-62. doi: 10.1002/anie.201102887. Epub 2011 Sep 22.
Abstract
A Membrane-bound Antiparallel Dimer of Rat Islet Amyloid Polypeptide IAPP, an amyloidogenic peptide linked to type 2 diabetes, forms a heterogeneous mixture of membrane-bound oligomers implicated in cytotoxicity and fibril formation. Structural characterization of these species has been a long-standing problem. Here, we examine the structure of a previously unrecognized antiparallel dimer of rat IAPP bound to anionic membrane Nanodiscs, using a novel combination of single-pair FRET and Rosetta model refinement.
摘要
一种结合了单对荧光共振能量转移（FRET）和罗赛塔模型精修的新型方法，用于研究此前未被识别的与阴离子膜纳米盘结合的大鼠胰岛淀粉样多肽（IAPP）的反平行二聚体。这种反平行二聚体是一种与 2 型糖尿病相关的淀粉样肽，可形成细胞毒性和纤维形成相关的混合性膜结合寡聚物。对这些物种的结构特征进行分析一直是一个长期存在的问题。
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Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity.胰岛淀粉样多肽表现出持续破坏膜完整性的能力。
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