Abstract
Amyloids constitute a class of protein and protein fragments believed to be involved in the pathologies associated with Alzheimer's, Parkinson's and Creutzfeldt-Jakob diseases. These proteins can self-assemble into unique fibrillar structures that are resistant to normal protein degradation. Interesting recent developments in the study of amyloid fibrils demonstrate that they bind carbon allotropes. In this study using single-walled carbon nanotube field-effect transistors (SWCNT-FETs), we show that the fibrillar form of Alzheimer's amyloid β (1–40) and (1–42) peptides specifically bind non-functionalized SWCNT in a saturable manner. Both peptides exhibited near identical binding curves with half-maximal binding concentrations of approximately 12 μg/ml. Binding of the peptides to SWCNTs was diminished by including dimethyl sulphoxide (DMSO) at concentrations that inhibits fibril formation. Lastly a monoclonal antibody (BAM-10), which binds to the N-terminal region of Alzheimer's amyloid fibrils, recognizes the amyloid peptides adhering to SWCNTs in the absence of DMSO, but not in the presence of 75% DMSO. Taken together, these results suggest that the fibrillar form of the Alzheimer's amyloid peptides are specifically binding to SWCNTs.
Highlights
Amyloidosis includes neuropathologies such as Alzheimer’s, Parkinson’s, Huntington’s and Creutzfeldt– Jakob disease [1, 2]
In the present study we examine the interactions of A 40 and Aβ42 peptides with single‐walled carbon nanotubes (SWCNTs) immobilized on silica wafers
To discern whether the fibrillar form of the peptides was responsible for the observed binding, we performed binding studies in the presence of dimethyl sulphoxide (DMSO). These results suggest that the fibrillar form of the peptides was binding to the SWCNT‐FET
Summary
Amyloidosis includes neuropathologies such as Alzheimer’s, Parkinson’s, Huntington’s and Creutzfeldt– Jakob disease [1, 2]. Many nanomaterials, such as quantum dots, fluorinated nanoparticles and TiO2 nanoparticles, have been shown to bind Aβ amyloids [17, 18] Manufactured carbon allotropes, such as fullerenes, graphite and multi‐ walled carbon nanotubes, have been shown to interact with some Aβ peptides [19,20,21]. Additions to the nanotubes can disrupt the sp bonds and compromise their electrical properties [36] To overcome this barrier, functionalization of the SWCNTs can utilize their hydrophobicity by treating them with reactive hydrophobic linker molecules such as pyrenebutyric acid N‐hydroxysuccinimide ester (pyrene‐NHS). These results indicate that the SWCNT‐FET can be used to examine the transition of amyloid peptides from monomeric forms to polymeric fibrils and perhaps to measure the concentration of fibrillar Aβ peptides in biological samples
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