Adsorption at Liquid Interfaces Induces Amyloid Fibril Bending and Ring Formation
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- 作者：Sophia Jordens ; Emily E. Riley ; Ivan Usov ; Lucio Isa ; Peter D. Olmsted ; Raffaele Mezzenga
- 刊名：ACS Nano
- 出版年：2014
- 出版时间：November 25, 2014
- 年：2014
- 卷：8
- 期：11
- 页码：11071-11079
- 全文大小：664K
- ISSN：1936-086X
文摘
Protein fibril accumulation at interfaces is an important step in many physiological processes and neurodegenerative diseases as well as in designing materials. Here we show, using 尾-lactoglobulin fibrils as a model, that semiflexible fibrils exposed to a surface do not possess the Gaussian distribution of curvatures characteristic for wormlike chains, but instead exhibit a spontaneous curvature, which can even lead to ring-like conformations. The long-lived presence of such rings is confirmed by atomic force microscopy, cryogenic scanning electron microscopy, and passive probe particle tracking at air鈥?and oil鈥搘ater interfaces. We reason that this spontaneous curvature is governed by structural characteristics on the molecular level and is to be expected when a chiral and polar fibril is placed in an inhomogeneous environment such as an interface. By testing 尾-lactoglobulin fibrils with varying average thicknesses, we conclude that fibril thickness plays a determining role in the propensity to form rings.