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Title: Identifying Cu( ii )–amyloid peptide binding intermediates in the early stages of aggregation by resonance Raman spectroscopy: a simulation study

Abstract

The aggregation of amyloid beta (Aβ) peptides plays a crucial role in the pathology and etiology of Alzheimer's disease. Experimental evidence shows that copper ion is an aggregation-prone species with the ability to coordinately bind to Aβ and further induce the formation of neurotoxic Aβ oligomers. However, the detailed structures of Cu(II)–Aβ complexes have not been illustrated, and the kinetics and dynamics of the Cu(II) binding are not well understood. Two Cu(II)–Aβ complexes have been proposed to exist under physiological conditions, and another two might exist at higher pH values. By using ab initio simulations for the spontaneous resonance Raman and time domain stimulated resonance Raman spectroscopy signals, we obtained the characteristic Raman vibronic features of each complex. Finally, these signals contain rich structural information with high temporal resolution, enabling the characterization of transient states during the fast Cu–Aβ binding and interconversion processes.

Authors:
ORCiD logo [1];  [2];  [3]; ORCiD logo [4];  [1]; ORCiD logo [1];  [1]
  1. China Univ. of Petroleum (East China), Qingdao (China). State Key Lab. of Heavy Oil Processing, Center for Bioengineering & Biotechnology
  2. Univ. of California, Irvine, CA (United States). Dept. of Chemistry
  3. China Univ. of Petroleum (East China), Qingdao (China). Dept. of Chemistry, College of Science
  4. Shandong Univ., Jinan (China). State Key Lab. of Crystal Materials
Publication Date:
Research Org.:
SLAC National Accelerator Lab., Menlo Park, CA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1425653
Grant/Contract Number:  
AC02-76SF00515; 2014M560587; 21403300; 21573129; 21773309
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Physical Chemistry Chemical Physics. PCCP (Print)
Additional Journal Information:
Journal Name: Physical Chemistry Chemical Physics. PCCP (Print); Journal Volume: 19; Journal Issue: 46; Journal ID: ISSN 1463-9076
Publisher:
Royal Society of Chemistry
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Ren, Hao, Zhang, Yu, Guo, Sibei, Lin, Na, Deng, Li, Yue, Tongtao, and Huang, Fang. Identifying Cu( ii )–amyloid peptide binding intermediates in the early stages of aggregation by resonance Raman spectroscopy: a simulation study. United States: N. p., 2017. Web. doi:10.1039/c7cp06206k.
Ren, Hao, Zhang, Yu, Guo, Sibei, Lin, Na, Deng, Li, Yue, Tongtao, & Huang, Fang. Identifying Cu( ii )–amyloid peptide binding intermediates in the early stages of aggregation by resonance Raman spectroscopy: a simulation study. United States. doi:10.1039/c7cp06206k.
Ren, Hao, Zhang, Yu, Guo, Sibei, Lin, Na, Deng, Li, Yue, Tongtao, and Huang, Fang. Tue . "Identifying Cu( ii )–amyloid peptide binding intermediates in the early stages of aggregation by resonance Raman spectroscopy: a simulation study". United States. doi:10.1039/c7cp06206k. https://www.osti.gov/servlets/purl/1425653.
@article{osti_1425653,
title = {Identifying Cu( ii )–amyloid peptide binding intermediates in the early stages of aggregation by resonance Raman spectroscopy: a simulation study},
author = {Ren, Hao and Zhang, Yu and Guo, Sibei and Lin, Na and Deng, Li and Yue, Tongtao and Huang, Fang},
abstractNote = {The aggregation of amyloid beta (Aβ) peptides plays a crucial role in the pathology and etiology of Alzheimer's disease. Experimental evidence shows that copper ion is an aggregation-prone species with the ability to coordinately bind to Aβ and further induce the formation of neurotoxic Aβ oligomers. However, the detailed structures of Cu(II)–Aβ complexes have not been illustrated, and the kinetics and dynamics of the Cu(II) binding are not well understood. Two Cu(II)–Aβ complexes have been proposed to exist under physiological conditions, and another two might exist at higher pH values. By using ab initio simulations for the spontaneous resonance Raman and time domain stimulated resonance Raman spectroscopy signals, we obtained the characteristic Raman vibronic features of each complex. Finally, these signals contain rich structural information with high temporal resolution, enabling the characterization of transient states during the fast Cu–Aβ binding and interconversion processes.},
doi = {10.1039/c7cp06206k},
journal = {Physical Chemistry Chemical Physics. PCCP (Print)},
number = 46,
volume = 19,
place = {United States},
year = {Tue Oct 31 00:00:00 EDT 2017},
month = {Tue Oct 31 00:00:00 EDT 2017}
}

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Works referenced in this record:

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Two-dimensional stimulated resonance Raman spectroscopy of molecules with broadband x-ray pulses
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