Issue 33, 2013

Heme prevents amyloid beta peptide aggregation through hydrophobic interaction based on molecular dynamics simulation

Abstract

Heme, which is abundant in hemoglobin and many other hemoproteins, is known to play an important role in electron transfer, oxygen transport, regulation of gene expression, and many other biological functions. With the belief that the aggregation of Aβ peptides forming higher order oligomers is one of the central pathological pathways in Alzheimer's disease, the formation of the Aβ–heme complex is essential as it inhibits Aβ aggregation and protects the neurons from degradation. In our studies, conventional molecular dynamics simulations were performed on the 1 Aβ + 1 heme and 2 Aβ + 4 hemes system, respectively, with the identification of several dominant binding motifs. We found that hydrophobic residues of the Aβ peptide have a high affinity to interact with heme instead of the histidine residue. We conclude that hydrophobic interaction plays a dominant role in the Aβ–heme complex formation which indirectly serves to physically prevent Aβ aggregation.

Graphical abstract: Heme prevents amyloid beta peptide aggregation through hydrophobic interaction based on molecular dynamics simulation

Supplementary files

Article information

Article type
Paper
Submitted
06 Jun 2013
Accepted
21 Jun 2013
First published
21 Jun 2013
This article is Open Access
Creative Commons BY-NC license

Phys. Chem. Chem. Phys., 2013,15, 14098-14106

Heme prevents amyloid beta peptide aggregation through hydrophobic interaction based on molecular dynamics simulation

L. N. Zhao, Y. Mu and L. Y. Chew, Phys. Chem. Chem. Phys., 2013, 15, 14098 DOI: 10.1039/C3CP52354C

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