| Summary: | 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 fieldeffect
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 g/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.
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