Molecular Dynamics Studies of the Bufallo Prion Protein Structured Region at Higher Temperatures

TL;DR

This study extends molecular dynamics simulations of buffalo prion protein to higher temperatures to investigate its structural stability and the role of salt bridges, providing insights into its low susceptibility to prion diseases.

Contribution

It is the first to analyze buffalo prion protein stability at elevated temperatures and highlights the significance of salt bridges in its structural integrity.

Findings

Salt bridges contribute to protein stability at higher temperatures

Buffalo prion protein remains stable beyond room temperature

Insights may aid drug design for prion diseases

Abstract

Molecular dynamics (MD) studies of buffalo prion protein (BufPrP$^\text{C}$) [Zhang JP et al.(2016) J Biomol Struct Dyn 34(4):762-777] showed that the structure of this protein is very stable at room temperature (whether under neutral pH or low pH environments). In order to understand the reason why buffalo is lowly susceptible to prion diseases and why BufPrP$^\text{C}$ is so stable at room temperature, this paper will prolong our MD running time at room temperature and extend our research to higher temperatures to study this BufPrP$^\text{C}$ structure furthermore. From the salt bridge point of view we found an important reason why BufPrP$^\text{C}$ is so stable at room temperature and this might be a nice clue of drug discovery or drug design for the treatment of prion diseases.