Amyloid formation of mutated Alzheimer's Aβ peptide 16-36 residues peptide and application in toxic lead and uranium ion binding

Aishwarya Natarajan; Late Ramakrishna Vadrevu; Aruna Jyothi Kora; Krishnan Rangan

doi:10.1039/d5na00228a

January 1, 2025Nanoscale AdvancesOpen Access

Amyloid formation of mutated Alzheimer's Aβ peptide 16-36 residues peptide and application in toxic lead and uranium ion binding

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Key Points

This peptide shows unique amyloid formation properties that may enhance binding to toxic materials.
The study highlights lead and uranium ion binding capabilities, indicating its potential as a biocompatible solution.
The mutated Alzheimer's peptide consists of 21 amino acids, contributing to its structural stability and function.
Implications for environmental health suggest that these findings may lead to innovative approaches in toxic ion remediation.

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Implication

Observational analysis reveals amyloid nanostructures bind toxic lead and uranium ions, suggesting potential environmental safeguards.

Abstract

A glutamic acid and arginine mutated 21 amino acid residue containing peptide developed based on Alzheimer's Aβ peptide shows propensity to form amyloid nanostructures which are used as biocompatible materials for toxic lead and uranium binding.

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Cite This Study

Natarajan et al. (2025) studied this question.

synapsesocial.com/papers/68c1b81254b1d3bfb60ec0cf https://doi.org/10.1039/d5na00228a

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Amyloid formation of mutated Alzheimer's Aβ peptide 16-36 residues peptide and application in toxic lead and uranium ion binding

Key Points

Ask about this paper

Implication

Abstract

Discussion

Cite This Study

Amyloid formation of mutated Alzheimer's Aβ peptide 16-36 residues peptide and application in toxic lead and uranium ion binding

Key Points

Ask about this paper

Implication

Abstract

Discussion

Cite This Study

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