Understanding structural characteristics of out-of-register hIAPP amyloid proteins via molecular dynamics
- Authors
- Baek, Inchul; Lee, Myeongsang; Na, Sungsoo
- Issue Date
- 2016
- Publisher
- ROYAL SOC CHEMISTRY
- Citation
- RSC ADVANCES, v.6, no.81, pp.77666 - 77672
- Indexed
- SCIE
SCOPUS
- Journal Title
- RSC ADVANCES
- Volume
- 6
- Number
- 81
- Start Page
- 77666
- End Page
- 77672
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/90411
- DOI
- 10.1039/c6ra19100b
- ISSN
- 2046-2069
- 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.
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Collections - College of Engineering > Department of Mechanical Engineering > 1. Journal Articles
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