Understanding structural characteristics of out-of-register hIAPP amyloid proteins

Via molecular dynamics

Inchul Baek, Myeongsang Lee, Sung Soo Na

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Amyloid oligomers are implicated in several neurodegenerative diseases; studies have shown oligomeric amyloids form fibrillary amyloids and have toxic effects on cell function. Several experimental and computational studies have investigated in-register amyloids and their characteristics. However, recently, out-of-register amyloid structures have been observed and their inherent weak structural stability exhibits higher toxicity under physiological conditions compared to that of in-register amyloids. Specifically, by varying the size of oligomeric hIAPP out-of-register structures from 4 layers to 20 layers, we successfully analyzed the structural characteristics of fibrillary out-of-register hIAPP; the critical structure size of out-of-register hIAPP is related to fibrillar growth from protofibrils. Through the structural analysis of out-of-register hIAPP, we shed light on the fibrillar growth mechanism of out-of-register hIAPP oligomer in detail.

Original languageEnglish
Pages (from-to)77666-77672
Number of pages7
JournalRSC Advances
Volume6
Issue number81
DOIs
Publication statusPublished - 2016 Jan 1

Fingerprint

Amyloidogenic Proteins
Amyloid
Molecular dynamics
Oligomers
Neurodegenerative diseases
Poisons
Structural analysis
Toxicity

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

Cite this

Understanding structural characteristics of out-of-register hIAPP amyloid proteins : Via molecular dynamics. / Baek, Inchul; Lee, Myeongsang; Na, Sung Soo.

In: RSC Advances, Vol. 6, No. 81, 01.01.2016, p. 77666-77672.

Research output: Contribution to journalArticle

@article{a848070eeac44efb84dd9382e0353f40,
title = "Understanding structural characteristics of out-of-register hIAPP amyloid proteins: Via molecular dynamics",
abstract = "Amyloid oligomers are implicated in several neurodegenerative diseases; studies have shown oligomeric amyloids form fibrillary amyloids and have toxic effects on cell function. Several experimental and computational studies have investigated in-register amyloids and their characteristics. However, recently, out-of-register amyloid structures have been observed and their inherent weak structural stability exhibits higher toxicity under physiological conditions compared to that of in-register amyloids. Specifically, by varying the size of oligomeric hIAPP out-of-register structures from 4 layers to 20 layers, we successfully analyzed the structural characteristics of fibrillary out-of-register hIAPP; the critical structure size of out-of-register hIAPP is related to fibrillar growth from protofibrils. Through the structural analysis of out-of-register hIAPP, we shed light on the fibrillar growth mechanism of out-of-register hIAPP oligomer in detail.",
author = "Inchul Baek and Myeongsang Lee and Na, {Sung Soo}",
year = "2016",
month = "1",
day = "1",
doi = "10.1039/c6ra19100b",
language = "English",
volume = "6",
pages = "77666--77672",
journal = "RSC Advances",
issn = "2046-2069",
publisher = "Royal Society of Chemistry",
number = "81",

}

TY - JOUR

T1 - Understanding structural characteristics of out-of-register hIAPP amyloid proteins

T2 - Via molecular dynamics

AU - Baek, Inchul

AU - Lee, Myeongsang

AU - Na, Sung Soo

PY - 2016/1/1

Y1 - 2016/1/1

N2 - Amyloid oligomers are implicated in several neurodegenerative diseases; studies have shown oligomeric amyloids form fibrillary amyloids and have toxic effects on cell function. Several experimental and computational studies have investigated in-register amyloids and their characteristics. However, recently, out-of-register amyloid structures have been observed and their inherent weak structural stability exhibits higher toxicity under physiological conditions compared to that of in-register amyloids. Specifically, by varying the size of oligomeric hIAPP out-of-register structures from 4 layers to 20 layers, we successfully analyzed the structural characteristics of fibrillary out-of-register hIAPP; the critical structure size of out-of-register hIAPP is related to fibrillar growth from protofibrils. Through the structural analysis of out-of-register hIAPP, we shed light on the fibrillar growth mechanism of out-of-register hIAPP oligomer in detail.

AB - Amyloid oligomers are implicated in several neurodegenerative diseases; studies have shown oligomeric amyloids form fibrillary amyloids and have toxic effects on cell function. Several experimental and computational studies have investigated in-register amyloids and their characteristics. However, recently, out-of-register amyloid structures have been observed and their inherent weak structural stability exhibits higher toxicity under physiological conditions compared to that of in-register amyloids. Specifically, by varying the size of oligomeric hIAPP out-of-register structures from 4 layers to 20 layers, we successfully analyzed the structural characteristics of fibrillary out-of-register hIAPP; the critical structure size of out-of-register hIAPP is related to fibrillar growth from protofibrils. Through the structural analysis of out-of-register hIAPP, we shed light on the fibrillar growth mechanism of out-of-register hIAPP oligomer in detail.

UR - http://www.scopus.com/inward/record.url?scp=85024364771&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85024364771&partnerID=8YFLogxK

U2 - 10.1039/c6ra19100b

DO - 10.1039/c6ra19100b

M3 - Article

VL - 6

SP - 77666

EP - 77672

JO - RSC Advances

JF - RSC Advances

SN - 2046-2069

IS - 81

ER -