Measurement of intrinsic properties of amyloid fibrils by the peak force QNM method

被引：173

作者：

Adamcik, Jozef ^{[1
]}

Lara, Cecile ^{[1
]}

Usov, Ivan ^{[1
]}

Jeong, Jae Sun ^{[2
]}

Ruggeri, Francesco S. ^{[2
]}

Dietler, Giovanni ^{[2
]}

Lashuel, Hilal A. ^{[3
]}

Hamley, Ian W. ^{[4
]}

Mezzenga, Raffaele ^{[1
]}

机构：

[1] ETH, Inst Food Nutr & Hlth, CH-8092 Zurich, Switzerland

[2] Ecole Polytech Fed Lausanne, Lab Phys Living Matter, CH-1015 Lausanne, Switzerland

[3] Ecole Polytech Fed Lausanne, Sch Life Sci, Brain Mind Inst, Lab Mol & Chem Biol Neurodegenerat, CH-1015 Lausanne, Switzerland

[4] Univ Reading, Dept Chem, Whiteknights Reading RG6 6AD, England

来源：

NANOSCALE | 2012年 / 4卷 / 15期

关键词：

GLOBULAR-PROTEINS; NANOMECHANICS; PROTOFIBRILS; MICROSCOPY; DISEASE;

D O I：

10.1039/c2nr30768e

中图分类号：

O6 [化学];

学科分类号：

070301 [无机化学];

摘要：

We report the investigation of the mechanical properties of different types of amyloid fibrils by the peak force quantitative nanomechanical (PF-QNM) technique. We demonstrate that this technique correctly measures the Young's modulus independent of the polymorphic state and the cross-sectional structural details of the fibrils, and we show that values for amyloid fibrils assembled from heptapeptides, alpha-synuclein, A beta(1-42), insulin, beta-lactoglobulin, lysozyme, ovalbumin, Tau protein and bovine serum albumin all fall in the range of 2-4 GPa.

引用

页码：4426 / 4429

页数：4

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