Investigation of the conformation of human prion protein in ethanol solution using molecular dynamics simulations

Abstract

When the conformation of protein is changed from its natural state to a misfolded state, some diseases will happen like prion disease. Prion diseases are a set of deadly neurodegenerative diseases caused by prion protein misfolding and aggregation. Monohydric alcohols have a strong influence on the structure of protein. However, whether monohydric alcohols inhibit amyloid fibrosis remains uncertain. Here, to elucidate the effect of ethanol on the structural stability of human prion protein, molecular dynamics simulations were employed to analyze the conformational changes and dynamics characteristics of human prion proteins at different temperatures. The results show that the extension of β-sheet occurs more easily and the α-helix is more easily disrupted at high temperatures. We found that ethanol can destroy the hydrophobic interactions and make the hydrogen bonds stable, which protects the secondary structure of the protein, especially at 500 K.

Communicated by Ramaswamy H. Sarma

Keywords:

• Prion protein
• ethanol
• elevated temperature
• principal component analysis
• molecular dynamics (MD) simulations

Disclosure statement

No potential conflict of interest was reported by the authors.

Additional information

Funding

This work was supported by the Foundation of Educational Committee of Jiangxi Province, China (Grant No.GJJ211112), the Fund for Distinguished Young Scholars of Jiangxi Science & Technology Normal University (Grant No.2015QN-BJRC002), the Jiangxi Key Laboratory of Flexible Electronics (Grant NO.2021BCD42004).