Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/103444
Title: Heme prevents amyloid beta peptide aggregation through hydrophobic interaction based on molecular dynamics simulation
Authors: Zhao, Li Na
Mu, Yuguang
Chew, Lock Yue
Keywords: DRNTU::Science::Biological sciences::Biophysics
Issue Date: 2013
Source: Zhao, L. N., Mu, Y., & Chew, L. Y. (2013). Heme prevents amyloid beta peptide aggregation through hydrophobic interaction based on molecular dynamics simulation. Physical chemistry chemical physics, 15(33), 14098-14106.
Series/Report no.: Physical chemistry chemical physics
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.
URI: https://hdl.handle.net/10356/103444
http://hdl.handle.net/10220/24524
DOI: http://dx.doi.org/10.1039/C3CP52354C
Rights: This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles
SPMS Journal Articles

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