, Volume 247, Issue 6, pp 523-530
Date: 09 Apr 2014

Probing of Various Physiologically Relevant Metals: Amyloid-β Peptide Interactions with a Lipid Membrane-Immobilized Protein Nanopore

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Abstract

One of the prevailing paradigms regarding the onset of Alzheimer’s disease endows metal ions with key roles in certain steps of the amyloid-β (Aβ) peptide aggregation cascade, through peptide conformational changes induced by metal binding. Herein, we focused on the truncated, more soluble Aβ1–16 peptide fragment from the human Aβ1–40, and demonstrated the utility of a sensing element based on the α-hemolysin (α-HL) protein to examine and compare at single-molecule level the interactions between such peptides and various metals. By using the same approach, we quantified Cu2+ and Zn2+ binding affinities to the Aβ1–16 fragment, whereas the statistical analysis of blockages induced by a single Aβ1–16 peptide on the current flow through an open α-HL pore show that the metal propensity to interacting with the peptide and entailing conformational changes obey the following order: Cu2+ > Zn2+ > Fe3+ > Al3+.

Alina Asandei and Sorana Iftemi have contributed equally to this work.
An erratum to this article can be found at http://dx.doi.org/10.1007/s00232-014-9667-7.