Identifying Polymorphs of Amyloid-β (1-40) Fibrils Using High-Resolution Atomic Force Microscopy

被引：7

作者：

Lin, Yi-Chih ^{[1
]}

Komatsu, Hiroaki ^{[3
,4
,5
]}

Ma, Jianqiang ^{[1
,2
]}

Axelsen, Paul H. ^{[3
,4
,5
]}

Fakhraai, Zahra ^{[1
]}

机构：

[1] Univ Penn, Dept Chem, 231 South 34th St, Philadelphia, PA 19104 USA

[2] Univ Penn, Ultrafast Opt Proc Lab, 231 South 34th St, Philadelphia, PA 19104 USA

[3] Univ Penn, Sch Med, Dept Pharmacol, Philadelphia, PA 19104 USA

[4] Univ Penn, Sch Med, Dept Biochem & Biophys, Philadelphia, PA 19104 USA

[5] Univ Penn, Sch Med, Dept Med Infect Dis, Philadelphia, PA 19104 USA

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2019年 / 123卷 / 49期

关键词：

MASS-PER-LENGTH; STRUCTURAL BASIS; QUATERNARY STRUCTURE; ALZHEIMERS; HETEROGENEITY; LEVEL;

D O I：

10.1021/acs.jpcb.9b07854

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Many amyloid-beta fibril preparations are highly polymorphic, and the conditions under which they are formed determine their morphology. This report describes the application of high-resolution atomic force microscopy (HR-AFM), combined with volume-per-length analysis, to define, identify, and quantify the structural components of polymorphic A beta fibril preparations. Volume-per-length analysis confirms that they are composed of discrete cross-beta filaments, and the analysis of HR-AFM images yields the number of striations in each fibril. Compared to mass-per-length analysis by electron microscopy, HR-AFM analysis yields narrower distributions, facilitating rapid and label-free quantitative morphological characterization of A beta fibril preparations.

引用

页码：10376 / 10383

页数：8

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