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...
Guardado en:
Autores principales: | , , , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2012
|
Materias: | |
Acceso en línea: | https://doaj.org/article/2e44d7e4452d4acd9b9d0c3562544a87 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:2e44d7e4452d4acd9b9d0c3562544a87 |
---|---|
record_format |
dspace |
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 |
work_keys_str_mv |
AT weiye insightintothestabilityofcrossbamyloidfibrilfromvealylshortpeptidewithmoleculardynamicssimulation AT yuechen insightintothestabilityofcrossbamyloidfibrilfromvealylshortpeptidewithmoleculardynamicssimulation AT weiwang insightintothestabilityofcrossbamyloidfibrilfromvealylshortpeptidewithmoleculardynamicssimulation AT qingfenyu insightintothestabilityofcrossbamyloidfibrilfromvealylshortpeptidewithmoleculardynamicssimulation AT yixueli insightintothestabilityofcrossbamyloidfibrilfromvealylshortpeptidewithmoleculardynamicssimulation AT jianzhang insightintothestabilityofcrossbamyloidfibrilfromvealylshortpeptidewithmoleculardynamicssimulation AT haifengchen insightintothestabilityofcrossbamyloidfibrilfromvealylshortpeptidewithmoleculardynamicssimulation |
_version_ |
1718423588164337664 |