Influence of Aromatic Residues on the Material Characteristics of Aβ Amyloid Protofibrils at the Atomic Scale

Hyun Joon Chang, Inchul Baek, Myeongsang Lee, Sung Soo Na

Research output: Contribution to journalArticle

13 Citations (Scopus)

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 languageEnglish
Pages (from-to)2403-2414
Number of pages12
JournalChemPhysChem
Volume16
Issue number11
DOIs
Publication statusPublished - 2015 Aug 1

Fingerprint

Amyloid
structural stability
Elastic Modulus
Molecular Dynamics Simulation
Fluorescence
Molecular dynamics
modulus of elasticity
Elastic moduli
molecular dynamics
fluorescence
causes
Computer simulation
simulation

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 journalArticle

Chang, Hyun Joon ; Baek, Inchul ; Lee, Myeongsang ; Na, Sung Soo. / Influence of Aromatic Residues on the Material Characteristics of Aβ Amyloid Protofibrils at the Atomic Scale. In: ChemPhysChem. 2015 ; Vol. 16, No. 11. pp. 2403-2414.
@article{1cad19fcbe0f4c9e81f1b6a9eb4a4327,
title = "Influence of Aromatic Residues on the Material Characteristics of Aβ Amyloid Protofibrils at the Atomic Scale",
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.",
keywords = "amyloid beta-peptides, mechanical properties, molecular dynamics, molecular modeling, stacking interactions",
author = "Chang, {Hyun Joon} and Inchul Baek and Myeongsang Lee and Na, {Sung Soo}",
year = "2015",
month = "8",
day = "1",
doi = "10.1002/cphc.201500244",
language = "English",
volume = "16",
pages = "2403--2414",
journal = "ChemPhysChem",
issn = "1439-4235",
publisher = "Wiley-VCH Verlag",
number = "11",

}

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

UR - http://www.scopus.com/inward/record.url?scp=84937969810&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84937969810&partnerID=8YFLogxK

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 -