Abstract
Amyloid fibrils, which cause a number of degenerative diseases, are insoluble under physiological conditions and are supported by native contacts. Recently, the effects of the aromatic residues on the Aβ amyloid protofibril were investigated in a ThT fluorescence study. However, the relationship between the material characteristics of the Aβ protofibril and its aromatic residues has not yet been investigated on the atomic scale. Here, we successfully constructed wild-type (WT) and mutated types of Aβ protofibrils by using molecular dynamics simulations. Through principle component analysis, we established the structural stability and vibrational characteristics of F20L Aβ protofibrils and compared them with WT and other mutated models such as F19L and F19LF20L. In addition, structural stability was assessed by calculating the elastic modulus, which showed that the F20L model has higher values than the other models studied. From our results, it is shown that aromatic residues influence the structural and material characteristics of Aβ protofibrils.
| Original language | English |
|---|---|
| Pages (from-to) | 2403-2414 |
| Number of pages | 12 |
| Journal | ChemPhysChem |
| Volume | 16 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - 2015 Aug 1 |
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Keywords
- amyloid beta-peptides
- mechanical properties
- molecular dynamics
- molecular modeling
- stacking interactions
ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Atomic and Molecular Physics, and Optics
Cite this
Influence of Aromatic Residues on the Material Characteristics of Aβ Amyloid Protofibrils at the Atomic Scale. / Chang, Hyun Joon; Baek, Inchul; Lee, Myeongsang; Na, Sung Soo.
In: ChemPhysChem, Vol. 16, No. 11, 01.08.2015, p. 2403-2414.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Influence of Aromatic Residues on the Material Characteristics of Aβ Amyloid Protofibrils at the Atomic Scale
AU - Chang, Hyun Joon
AU - Baek, Inchul
AU - Lee, Myeongsang
AU - Na, Sung Soo
PY - 2015/8/1
Y1 - 2015/8/1
N2 - Amyloid fibrils, which cause a number of degenerative diseases, are insoluble under physiological conditions and are supported by native contacts. Recently, the effects of the aromatic residues on the Aβ amyloid protofibril were investigated in a ThT fluorescence study. However, the relationship between the material characteristics of the Aβ protofibril and its aromatic residues has not yet been investigated on the atomic scale. Here, we successfully constructed wild-type (WT) and mutated types of Aβ protofibrils by using molecular dynamics simulations. Through principle component analysis, we established the structural stability and vibrational characteristics of F20L Aβ protofibrils and compared them with WT and other mutated models such as F19L and F19LF20L. In addition, structural stability was assessed by calculating the elastic modulus, which showed that the F20L model has higher values than the other models studied. From our results, it is shown that aromatic residues influence the structural and material characteristics of Aβ protofibrils.
AB - Amyloid fibrils, which cause a number of degenerative diseases, are insoluble under physiological conditions and are supported by native contacts. Recently, the effects of the aromatic residues on the Aβ amyloid protofibril were investigated in a ThT fluorescence study. However, the relationship between the material characteristics of the Aβ protofibril and its aromatic residues has not yet been investigated on the atomic scale. Here, we successfully constructed wild-type (WT) and mutated types of Aβ protofibrils by using molecular dynamics simulations. Through principle component analysis, we established the structural stability and vibrational characteristics of F20L Aβ protofibrils and compared them with WT and other mutated models such as F19L and F19LF20L. In addition, structural stability was assessed by calculating the elastic modulus, which showed that the F20L model has higher values than the other models studied. From our results, it is shown that aromatic residues influence the structural and material characteristics of Aβ protofibrils.
KW - amyloid beta-peptides
KW - mechanical properties
KW - molecular dynamics
KW - molecular modeling
KW - stacking interactions
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U2 - 10.1002/cphc.201500244
DO - 10.1002/cphc.201500244
M3 - Article
VL - 16
SP - 2403
EP - 2414
JO - ChemPhysChem
JF - ChemPhysChem
SN - 1439-4235
IS - 11
ER -