Mechanical and vibrational characterization of amyloid-like HET-s nanosheets based on the skewed plate theory

Hyun Joon Chang, Myeongsang Lee, Jae In Kim, Gwonchan Yoon, Sung Soo Na

Research output: Contribution to journalArticle

Abstract

Pathological amyloidogenic prion proteins have a toxic effect on functional cells in the human cerebrum because of poor degradability and the tendency to accumulate in an uncontrolled manner under physiological conditions. HET-s, a fungal prion protein, is known to undergo conformational variations from fibrillar to nanosheet structures during a change from low to high pH conditions. It has been said that this conformational change can lead to self-propagation by nucleating on the lateral surface of singlet fibrils. Efforts have been made toward the mechanical characterization of fibrillar amyloids, but a global understanding of amyloid-like HET-s nanosheet structures is lacking. In this study, we analyzed the mechanical and vibrational characteristics of the skewed HET-s nanosheet structures that developed under neutral pH conditions by performing various molecular dynamics simulations. By applying the skewed plate theory to HET-s nanosheets for various length scales with numerous pores inside the structures, we found that the skewed HET-s nanosheet structure has mechanical properties comparable to those of previously reported biological film materials and nanomaterials. Considering the inherent characteristics of structural stability, our observation provides valuable and detailed structural information on skewed amyloid-like HET-s nanosheets.

Original languageEnglish
Pages (from-to)11492-11501
Number of pages10
JournalPhysical Chemistry Chemical Physics
Volume19
Issue number18
DOIs
Publication statusPublished - 2017

Fingerprint

plate theory
Nanosheets
Amyloid
cerebrum
self propagation
proteins
Amyloidogenic Proteins
Fungal Proteins
Nanostructures
Poisons
Cerebrum
structural stability
Molecular Dynamics Simulation
tendencies
Observation
mechanical properties
molecular dynamics
porosity
cells
Nanostructured materials

ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

Cite this

Mechanical and vibrational characterization of amyloid-like HET-s nanosheets based on the skewed plate theory. / Chang, Hyun Joon; Lee, Myeongsang; Kim, Jae In; Yoon, Gwonchan; Na, Sung Soo.

In: Physical Chemistry Chemical Physics, Vol. 19, No. 18, 2017, p. 11492-11501.

Research output: Contribution to journalArticle

Chang, Hyun Joon ; Lee, Myeongsang ; Kim, Jae In ; Yoon, Gwonchan ; Na, Sung Soo. / Mechanical and vibrational characterization of amyloid-like HET-s nanosheets based on the skewed plate theory. In: Physical Chemistry Chemical Physics. 2017 ; Vol. 19, No. 18. pp. 11492-11501.
@article{14ae59339c6a434a915e57b3b770a297,
title = "Mechanical and vibrational characterization of amyloid-like HET-s nanosheets based on the skewed plate theory",
abstract = "Pathological amyloidogenic prion proteins have a toxic effect on functional cells in the human cerebrum because of poor degradability and the tendency to accumulate in an uncontrolled manner under physiological conditions. HET-s, a fungal prion protein, is known to undergo conformational variations from fibrillar to nanosheet structures during a change from low to high pH conditions. It has been said that this conformational change can lead to self-propagation by nucleating on the lateral surface of singlet fibrils. Efforts have been made toward the mechanical characterization of fibrillar amyloids, but a global understanding of amyloid-like HET-s nanosheet structures is lacking. In this study, we analyzed the mechanical and vibrational characteristics of the skewed HET-s nanosheet structures that developed under neutral pH conditions by performing various molecular dynamics simulations. By applying the skewed plate theory to HET-s nanosheets for various length scales with numerous pores inside the structures, we found that the skewed HET-s nanosheet structure has mechanical properties comparable to those of previously reported biological film materials and nanomaterials. Considering the inherent characteristics of structural stability, our observation provides valuable and detailed structural information on skewed amyloid-like HET-s nanosheets.",
author = "Chang, {Hyun Joon} and Myeongsang Lee and Kim, {Jae In} and Gwonchan Yoon and Na, {Sung Soo}",
year = "2017",
doi = "10.1039/c7cp01418j",
language = "English",
volume = "19",
pages = "11492--11501",
journal = "Physical Chemistry Chemical Physics",
issn = "1463-9076",
publisher = "Royal Society of Chemistry",
number = "18",

}

TY - JOUR

T1 - Mechanical and vibrational characterization of amyloid-like HET-s nanosheets based on the skewed plate theory

AU - Chang, Hyun Joon

AU - Lee, Myeongsang

AU - Kim, Jae In

AU - Yoon, Gwonchan

AU - Na, Sung Soo

PY - 2017

Y1 - 2017

N2 - Pathological amyloidogenic prion proteins have a toxic effect on functional cells in the human cerebrum because of poor degradability and the tendency to accumulate in an uncontrolled manner under physiological conditions. HET-s, a fungal prion protein, is known to undergo conformational variations from fibrillar to nanosheet structures during a change from low to high pH conditions. It has been said that this conformational change can lead to self-propagation by nucleating on the lateral surface of singlet fibrils. Efforts have been made toward the mechanical characterization of fibrillar amyloids, but a global understanding of amyloid-like HET-s nanosheet structures is lacking. In this study, we analyzed the mechanical and vibrational characteristics of the skewed HET-s nanosheet structures that developed under neutral pH conditions by performing various molecular dynamics simulations. By applying the skewed plate theory to HET-s nanosheets for various length scales with numerous pores inside the structures, we found that the skewed HET-s nanosheet structure has mechanical properties comparable to those of previously reported biological film materials and nanomaterials. Considering the inherent characteristics of structural stability, our observation provides valuable and detailed structural information on skewed amyloid-like HET-s nanosheets.

AB - Pathological amyloidogenic prion proteins have a toxic effect on functional cells in the human cerebrum because of poor degradability and the tendency to accumulate in an uncontrolled manner under physiological conditions. HET-s, a fungal prion protein, is known to undergo conformational variations from fibrillar to nanosheet structures during a change from low to high pH conditions. It has been said that this conformational change can lead to self-propagation by nucleating on the lateral surface of singlet fibrils. Efforts have been made toward the mechanical characterization of fibrillar amyloids, but a global understanding of amyloid-like HET-s nanosheet structures is lacking. In this study, we analyzed the mechanical and vibrational characteristics of the skewed HET-s nanosheet structures that developed under neutral pH conditions by performing various molecular dynamics simulations. By applying the skewed plate theory to HET-s nanosheets for various length scales with numerous pores inside the structures, we found that the skewed HET-s nanosheet structure has mechanical properties comparable to those of previously reported biological film materials and nanomaterials. Considering the inherent characteristics of structural stability, our observation provides valuable and detailed structural information on skewed amyloid-like HET-s nanosheets.

UR - http://www.scopus.com/inward/record.url?scp=85024369717&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85024369717&partnerID=8YFLogxK

U2 - 10.1039/c7cp01418j

DO - 10.1039/c7cp01418j

M3 - Article

C2 - 28425516

AN - SCOPUS:85024369717

VL - 19

SP - 11492

EP - 11501

JO - Physical Chemistry Chemical Physics

JF - Physical Chemistry Chemical Physics

SN - 1463-9076

IS - 18

ER -