Oriented epitaxial growth of amyloid fibrils of the N27C mutant beta 25-35 peptide

European Biophysics Journal : EBJ
Arpád KarsaiMiklós S Z Kellermayer

Abstract

Amyloid fibrils are present in the extracellular space of various tissues in neurodegenerative and protein misfolding diseases. Amyloid fibrils may be used in nanotechnology applications, because of their self-assembly properties and stability, if their growth and orientation can be controlled. Recently, we have shown that amyloid beta 25-35 (A beta 25-35) forms a highly oriented, K(+)-dependent network on mica. Here, we analyzed the properties of A beta 25-35_N27C, the cysteine residue of which may be used for subsequent chemical modifications. We find that A beta 25-35_N27C forms epitaxially growing fibrils on mica, which evolve into a trigonally oriented branched network. The binding is apparently more sensitive to cation concentration than that of the wild-type peptide. By nanomanipulating A beta 25-35_N27C fibrils with a gold-coated AFM tip, we show that the sulfhydryl of Cys27 is reactive and accessible from the solution. The oriented network of A beta 25-35_N27C fibrils can therefore be specifically labeled and may be used for constructing nanobiotechnological devices.

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Citations

Jan 12, 2013·Cell Biochemistry and Biophysics·Olga N KorolevaValeriy L Drutsa
Jun 28, 2011·Nanomedicine : Nanotechnology, Biology, and Medicine·Evgeniy V DubrovinValeriy L Drutsa
Jun 24, 2010·Protein Science : a Publication of the Protein Society·Yuebiao ShengP Chen
Apr 20, 2011·Journal of Molecular Recognition : JMR·Unige MurvaiMiklós S Z Kellermayer
Apr 20, 2011·Journal of Molecular Recognition : JMR·Ricardo H PiresMiklós S Z Kellermayer
Jul 26, 2014·Physical Review Letters·Wonmuk Hwang, Esma Eryilmaz
Jul 12, 2011·Langmuir : the ACS Journal of Surfaces and Colloids·Wee Wen Leow, Wonmuk Hwang
Feb 28, 2014·ACS Nano·Céline CharbonneauMartien A Cohen Stuart

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