RESEARCH ARTICLE

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

Jiapu Zhang1 , * Open Modal Authors Info & Affiliations
The Open Bioinformatics Journal 31 December 2020 RESEARCH ARTICLE DOI: 10.2174/1875036202013010129

Abstract

Background:

Molecular Dynamics (MD) studies of Buffalo Prion Protein (BufPrPC) (J Biomol Struct Dyn 2016; 34(4): 762-77) showed that the structure of this protein is very stable at room temperature (whether under neutral pH or low pH environments).

Methods:

In order to understand the reason why buffalo is resistant to prion diseases and why BufPrPC 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 BufPrPC structure furthermore.

Results:

From the salt bridge point of view, we found an important reason why BufPrPC is so stable at room temperature; this might be a nice clue of drug discovery or drug design for the treatment of prion diseases.

Conclusion:

In conclusion, this brief article talks about the MD results of BufPrP at different temperatures and presents a clue to seek the reasons for the conversion from normal cellular prion protein (PrPC) to diseased infectious prions (PrPSc). This should be very useful for the goals of medicinal chemistry in prion diseases research fields.

Keywords: Buffalo PrP, Stable protein structure, Room temperature, Higher temperatures, Drug discovery, Prion diseases.
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