Insight into the stability of cross-β amyloid fibril from VEALYL short peptide with molecular dynamics simulation.

Amyloid fibrils are found in many fatal neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, type II diabetes, and prion disease. The VEALYL short peptide from insulin has been confirmed to aggregate amyloid-like fibrils. However, the aggregation mechanism of amyloi...

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Autores principales: Wei Ye, Yue Chen, Wei Wang, Qingfen Yu, Yixue Li, Jian Zhang, Hai-Feng Chen
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Publicado: Public Library of Science (PLoS) 2012
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spelling oai:doaj.org-article:2e44d7e4452d4acd9b9d0c3562544a872021-11-18T07:19:12ZInsight into the stability of cross-β amyloid fibril from VEALYL short peptide with molecular dynamics simulation.1932-620310.1371/journal.pone.0036382https://doaj.org/article/2e44d7e4452d4acd9b9d0c3562544a872012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22590535/?tool=EBIhttps://doaj.org/toc/1932-6203Amyloid fibrils are found in many fatal neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, type II diabetes, and prion disease. The VEALYL short peptide from insulin has been confirmed to aggregate amyloid-like fibrils. However, the aggregation mechanism of amyloid fibril is poorly understood. Here, we utilized molecular dynamics simulation to analyse the stability of VEALYL hexamer. The statistical results indicate that hydrophobic residues play key roles in stabilizing VEALYL hexamer. Single point and two linkage mutants confirmed that Val1, Leu4, and Tyr5 of VEALYL are key residues. The consistency of the results for the VEALYL oligomer suggests that the intermediate states might be trimer (3-0) and pentamer(3-2). These results can help us to obtain an insight into the aggregation mechanism of amyloid fibril. These methods can be used to study the stability of amyloid fibril from other short peptides.Wei YeYue ChenWei WangQingfen YuYixue LiJian ZhangHai-Feng ChenPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 5, p e36382 (2012)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Wei Ye
Yue Chen
Wei Wang
Qingfen Yu
Yixue Li
Jian Zhang
Hai-Feng Chen
Insight into the stability of cross-β amyloid fibril from VEALYL short peptide with molecular dynamics simulation.
description Amyloid fibrils are found in many fatal neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, type II diabetes, and prion disease. The VEALYL short peptide from insulin has been confirmed to aggregate amyloid-like fibrils. However, the aggregation mechanism of amyloid fibril is poorly understood. Here, we utilized molecular dynamics simulation to analyse the stability of VEALYL hexamer. The statistical results indicate that hydrophobic residues play key roles in stabilizing VEALYL hexamer. Single point and two linkage mutants confirmed that Val1, Leu4, and Tyr5 of VEALYL are key residues. The consistency of the results for the VEALYL oligomer suggests that the intermediate states might be trimer (3-0) and pentamer(3-2). These results can help us to obtain an insight into the aggregation mechanism of amyloid fibril. These methods can be used to study the stability of amyloid fibril from other short peptides.
format article
author Wei Ye
Yue Chen
Wei Wang
Qingfen Yu
Yixue Li
Jian Zhang
Hai-Feng Chen
author_facet Wei Ye
Yue Chen
Wei Wang
Qingfen Yu
Yixue Li
Jian Zhang
Hai-Feng Chen
author_sort Wei Ye
title Insight into the stability of cross-β amyloid fibril from VEALYL short peptide with molecular dynamics simulation.
title_short Insight into the stability of cross-β amyloid fibril from VEALYL short peptide with molecular dynamics simulation.
title_full Insight into the stability of cross-β amyloid fibril from VEALYL short peptide with molecular dynamics simulation.
title_fullStr Insight into the stability of cross-β amyloid fibril from VEALYL short peptide with molecular dynamics simulation.
title_full_unstemmed Insight into the stability of cross-β amyloid fibril from VEALYL short peptide with molecular dynamics simulation.
title_sort insight into the stability of cross-β amyloid fibril from vealyl short peptide with molecular dynamics simulation.
publisher Public Library of Science (PLoS)
publishDate 2012
url https://doaj.org/article/2e44d7e4452d4acd9b9d0c3562544a87
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AT weiwang insightintothestabilityofcrossbamyloidfibrilfromvealylshortpeptidewithmoleculardynamicssimulation
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