EPR spectroscopy reveals different Cu( ii ) coordination in APP ₁₄₂–₁₇₂ and APP ₁₄₅–₁₇₀ peptide fragments of amyloid precursor protein

Liya Xu; Jian Kuang; Ao Liu; Lianghuan Liao; Lu Yu; Changlin Tian

doi:10.1039/d6ra00647g

January 1, 2026RSC AdvancesOpen Access

EPR spectroscopy reveals different Cu( ii ) coordination in APP ₁₄₂–₁₇₂ and APP ₁₄₅–₁₇₀ peptide fragments of amyloid precursor protein

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Key Points

This research aims to investigate how subtle sequence variations in APP peptides affect copper coordination.
Utilized EPR spectroscopy to analyze copper coordination in APP peptide fragments.
Compared the coordination modes between APP 142–172 and APP 145–170.
Identified differences in redox activity associated with each peptide fragment.
APP 142–172 peptide exhibits a redox-active N2O2 configuration.
APP 145–170 peptide shows both redox-active N2O2 and redox-silent 4N coordination modes.

Implication

EPR spectroscopy reveals copper coordination differences in APP peptides, indicating redox activity variations.

Abstract

Subtle APP sequence variations influence copper coordination: APP 142–172 adopts redox-active N 2 O 2 configuration while APP 145–170 exhibits both redox-active N 2 O 2 and redox-silent 4N modes.

Discussion

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Cite This Study

Xu et al. (2026) studied this question.

synapsesocial.com/papers/69be37096e48c4981c6765f2 https://doi.org/10.1039/d6ra00647g

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EPR spectroscopy reveals different Cu( ii ) coordination in APP ₁₄₂–₁₇₂ and APP ₁₄₅–₁₇₀ peptide fragments of amyloid precursor protein

Key Points

Implication

Abstract

Discussion

Cite This Study

EPR spectroscopy reveals different Cu( ii ) coordination in APP ₁₄₂–₁₇₂ and APP ₁₄₅–₁₇₀ peptide fragments of amyloid precursor protein

Key Points

Implication

Abstract

Discussion

Cite This Study

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