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Updated: Sep 30, 2025

Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
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Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores

Published on: April 5, 2022

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Simultaneous binding of heme and Cu with amyloid β peptides: active site and reactivities

Arnab Kumar Nath1, Somdatta Ghosh Dey1

  • 1School of Chemical Sciences, Indian Association for the Cultivation of Science, 2A & 2B, Raja S. C. Mullick Road, Jadavpur, Kolkata 700032, India. icsgd@iacs.res.in.

Dalton Transactions (Cambridge, England : 2003)
|March 10, 2022
PubMed

Insights

Alzheimer's disease (AD) involves amyloid plaques with copper (Cu) and heme. This review explores the heme-Cu-Aβ complex, detailing its properties and reactions with small molecules like oxygen and nitric oxide.

Area of Science:

  • Biochemistry
  • Neuroscience
  • Metalloprotein chemistry

Background:

  • Alzheimer's disease (AD) is characterized by amyloid plaques.
  • These plaques show increased copper (Cu) and heme deposition.
  • Heme and Cu interact with amyloid-beta (Aβ) in AD pathology.

Purpose of the Study:

  • To review the properties of the heme-Cu-Aβ complex.
  • To discuss the complex's interactions with small molecules.
  • To explore the role of metal-cofactor binding in AD.

Main Methods:

  • Spectroscopic analysis of heme-Cu-Aβ complex.
  • Electrochemical studies of the complex.
  • Investigation of reactivity with O2, NO, and NO2-.

Main Results:

  • Heme and Cu bind separately and together with Aβ.
  • The heme-Cu-Aβ complex exhibits distinct electronic and spectroscopic properties.
  • The complex shows reactivity with oxygen, nitric oxide, and nitrite.

Conclusions:

  • The heme-Cu-Aβ complex is a relevant species in Alzheimer's disease.
  • Understanding its properties and reactivity offers insights into AD pathogenesis.
  • Metal-cofactor interactions in amyloid plaques are crucial for AD.

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