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

Jiapu Zhang

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.

Highlights

Unlike bacteria and viruses, which are based on DNA and RNA, prions are unique as disease-causing agents since they are misfolded proteins
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 Molecular Dynamics (MD) running time at room temperature and extend our research to higher temperatures to study this BufPrPC structure, as presented in the Methods and Materials section
In the section of Results and Discussion, we will analyze our MD computational results and discuss the reason why BufPrPC is so stable at room temperature

Summary

Introduction

Unlike bacteria and viruses, which are based on DNA and RNA, prions are unique as disease-causing agents since they are misfolded proteins. Prions attack the nervous system of the organism, causing an incurable, fatal deterioration of the brain and nervous system until death occurs. Some examples of these diseases are mad cow disease in cattle, chronic wasting disease in deer and elk, and Creutzfeldt-Jakob disease in humans. Not every species is affected by prion diseases. Water buffalo is a species being resistant to prion diseases. 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

Results

Conclusion