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

10Citations
Citations of this article
35Readers
Mendeley users who have this article in their library.

Abstract

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. © 2012 Ye et al.

Cite

CITATION STYLE

APA

Ye, W., Chen, Y., Wang, W., Yu, Q., Li, Y., Zhang, J., & Chen, H. F. (2012). Insight into the stability of cross-β amyloid fibril from VEALYL short peptide with molecular dynamics simulation. PLoS ONE, 7(5). https://doi.org/10.1371/journal.pone.0036382

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free