Authors: Jeongjin Lee Junsu Park Byoung Kyu Kwak Inhee Choi Younghun Kim Kyunghee Choi Jongheop Yi
Publish Date: 2010/10/15
Volume: 28, Issue: 1, Pages: 184-188
Abstract
The effect of the properties of a nanostructured gold surface nanoAu surface on the aggregation of Amyloid β1–40 Aβ40 was investigated A nanoAu surface in the form of immobilized nanoparticles was prepared by using a thermal evaporator resulting in the formation of nanosized clusters with sizes less than 10 nm When Aβ40 was incubated with the nanoAu surface abnormally largesized tubular aggregates were formed on the surface and typical fibril formation was suppressed in the solution This abnormally large tubular structure represents a novel type of Aβ40 aggregate In the absence of the nanoAu surface the diameters of the Aβ40 fibrils were less than 10 nm However the height of the tubular aggregates formed on a nanoAu surface was 80–100 nm Such largesized aggregates of Aβ40 have not been reported in previous studies dealing with interactions of suspended nanoparticles with proteins This can be attributed to differences in the aggregation mechanism between immobilized and suspended nanoparticles The formation of Aβ40 aggregates by nanoAu surface will provide the possible mechanism for abnormal fibril formation
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