The structural study of copper-binding peptides: Implication in the aggregation of amyloid-β peptides

Ren Jie Lin, Tzyy Rong Jinn, Soonmin Jang, Fur Der Mai, Feng Yin Li

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

There is evidence that copper is bound to amyloid-β peptide (Aβ) in senile plaque of Alzheimer's disease. Copper also plays a role in the neurotoxicity of the Aβ aggregates associated with free radical damage. In this study, we used L-histidyl-L-histidine peptide (di-histidine) to represent Aβ along with ab initio calculation to characterize the probable coordination between Cu(II) and Aβs to explore the Aβ aggregate structures. Sixteen models of copper-di-histidine complexes were proposed to investigate the copper-induced aggregation of Aβs through copper ionic coordination. All structures of the proposed models were optimized at the M05-2X/LanL2DZ level, and an Aβ aggregation formation mechanism was proposed.

Original languageEnglish
Pages (from-to)891-897
Number of pages7
JournalJournal of the Chinese Chemical Society
Volume60
Issue number7
DOIs
Publication statusPublished - 2013

Keywords

  • Amyloid aggregation
  • Amyloid-β peptide
  • Density functional theory
  • Metal chelation

ASJC Scopus subject areas

  • Chemistry(all)

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