Institute of Biological Chemistry, Academia Sinica, No. 128, Section 2, Academia Road, Nankang, Taipei 115, Taiwan.
Institute of Biochemical Sciences, National Taiwan University, No. 1, Section 4, Roosevelt Road, Taipei 106, Taiwan.
J Am Chem Soc. 2022 Aug 3;144(30):13888-13894. doi: 10.1021/jacs.2c05479. Epub 2022 Jul 20.
Fibrils of the hamster prion peptide (sHaPrP, sequence 108-144) were prepared in an acidic solution, and their structure was solved by cryogenic electron microscopy with a resolution of 2.23 Å based on the gold-standard Fourier shell correlation (FSC) curve. The fibril has a novel architecture that has never been found in other amyloid fibrils. Each fibril is assembled by four protofilaments (PFs) and has an ordered water channel in the center. Each protofilament contains three β-strands (125-130, 133-135, and 138-141) arranged in an "R"-shaped construct. The structural data indicate that these three β-strand segments are the most amyloidogenic region of the prion peptide/protein and might be the site of nucleation during fibrillization under conditions without denaturants.
仓鼠朊病毒肽（sHaPrP，序列 108-144）的原纤维在酸性溶液中制备，并基于金标准傅里叶壳相关（FSC）曲线，通过低温电子显微镜以 2.23 Å 的分辨率解析其结构。该纤维具有一种新颖的结构，从未在其他淀粉样纤维中发现过。每条纤维由四个原纤维（PFs）组装而成，中心有一个有序的水通道。每个原纤维包含三个β-链（125-130、133-135 和 138-141），排列成“R”形结构。结构数据表明，这三个β-链段是朊病毒肽/蛋白最具淀粉样的区域，并且在没有变性剂的条件下，在纤维化过程中可能是成核的部位。
