ArticleThe Journal of membrane biology2014
Probing of various physiologically relevant metals-amyloid-β peptide interactions with a lipid membrane-immobilized protein nanopore [corrected].
Article in The Journal of membrane biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 28 citations in OpenAlex.
- Pioneering Role of Nanopore Single-Molecule Sensing in Environmental and Food Surveillance.Biosensors · 2025Review
- Characterizing Prion-Like Protein Aggregation: Emerging Nanopore-Based Approaches.Small methods · 2024Review
- Classification and applications of nanomaterialsHeliyon · 2024Review
- Probing the Hepatitis B Virus E-Antigen with a Nanopore Sensor Based on Collisional Events Analysis.Biosensors · 2022Article
- Nanopore detection of metal ions: Current status and future directions.Small methods · 2020Article
- Biomedical diagnosis perspective of epigenetic detections using alpha-hemolysin nanopore.AIMS materials science · 2015Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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 Cu(2+) and Zn(2+) 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: Cu(2+) > Zn(2+) > Fe(3+) > Al(3+).
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.