纤维
淀粉样纤维
生物物理学
原子力显微镜
静电学
结晶学
化学物理
离子强度
材料科学
离子键合
胶原纤维
化学
纳米技术
淀粉样β
离子
水溶液
生物
病理
物理化学
有机化学
疾病
医学
作者
Jozef Adamčík,Raffaele Mezzenga
出处
期刊:Soft Matter
[The Royal Society of Chemistry]
日期:2011-01-01
卷期号:7 (11): 5437-5437
被引量:143
摘要
We present compelling experimental evidence supported by theoretical arguments demonstrating that the periodic twisting pitch in protein amyloid fibrils arises from the fine balance between competing electrostatic energy and torsional elastic energy stored along the fibrils contour length. To construct the present picture we have used increasing ionic strengths to progressively screen the electrostatic interactions and observed the corresponding pitch variations in mature β-lactoglobulin amyloid fibrils using single-molecule atomic force microscopy (AFM). Because the ionic strength is changed afterfibrils formation, this does not affect the mechanism by which fibrils grow up to their mature structure. For each individual population of the multi-stranded fibrils family, the pitch is found to increase systematically with the salt content, leading to the gradual untwisting of the fibrils and to the establishment of a controllable pitch up to virtually infinite values.
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