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JBIC Journal of Biological Inorganic Chemistry

, Volume 24, Issue 8, pp 1245–1259 | Cite as

Active-site environment of Cu bound amyloid β and amylin peptides

  • Ishita Pal
  • Madhuparna Roy
  • Somdatta Ghosh DeyEmail author
Mini Review
Part of the following topical collections:
  1. Metal Ions and Degenerative Diseases

Abstract

Alzheimer’s disease (AD) and Type 2 Diabetes mellitus (T2Dm), two of the most common amyloidogenic diseases. They share a common pathological symptom, i.e., the formation of amyloid deposits comprised of amyloid β and amylin peptides, respectively. Autopsy of brains of AD-affected patients shows the presence of abnormally high concentrations of Cu in the deposited amyloid β plaques, while a significantly higher level of Cu is found in the serum of patients suffering from T2Dm. These invoke that Cu might play a crucial role in the onset of both AD and T2Dm. In fact, Cu is found to bind amyloid β as well as amylin relevant to AD and T2Dm, respectively. Cu–Aβ and Cu–amylin in their reduced states can generate partially reduced oxygen species (PROS) on reaction with O2 which leads to oxidative stress in the brain and in the pancreas, respectively. However, the pathway of O2 reduction is quite different for the two complexes. Moreover, the use of various spectroscopic techniques such as absorption, EPR, and CD involving native and site-directed mutants of the peptides show that their active-site environments are also dissimilar. Here, we have discussed the different aspects of Cu–Aβ and Cu–amylin complexes including their pH-dependent coordination environments and their reactivity towards O2 which may be responsible for the oxidative stress associated with the two diseases. This depicts the significance of the Cu bound peptide complexes in the context of AD and T2Dm.

Graphic abstract

Keywords

Electron paramagnetic resonance Ligand binding Metallo-peptide Reactivity Spectroscopy COPPER 

Notes

Acknowledgements

We thank DST, SERB India for financial support (Grants EMR/2014/000392). Ishita Pal thanks UGC and Madhuparna Roy thanks CSIR for research fellowship.

Compliance with ethical standards

Conflicts of interest

There are no conflicts to declare.

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Copyright information

© Society for Biological Inorganic Chemistry (SBIC) 2019

Authors and Affiliations

  • Ishita Pal
    • 1
  • Madhuparna Roy
    • 1
  • Somdatta Ghosh Dey
    • 1
    Email author
  1. 1.Indian Association for the Cultivation of Science, School of Chemical SciencesKolkataIndia

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