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

Zhang, Jiapu

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

Jiapu Zhang^{1, *}

¹ Centre of Informatics and Applied Optimisation, Federation University Australia, Mount Helen Campus, Ballarat, Victoria 3353, Australia

Article Information

Identifiers and Pagination:

Year: 2020
Volume: 13
First Page: 129
Last Page: 136
Publisher ID: TOBIOIJ-13-129
DOI: 10.2174/1875036202013010129

Article History:

Received Date: 11/8/2020
Revision Received Date: 7/12/2020
Acceptance Date: 14/12/2020
Electronic publication date: 31/12/2020
Collection year: 2020

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© 2020 Jiapu Zhang.

open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: https://creativecommons.org/licenses/by/4.0/legalcode. This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

^* Address correspondence to this author at Centre of Informatics and Applied Optimisation, Federation University Australia, Mount Helen Campus, Ballarat, Victoria 3353, Australia; Tel: +61-3-5327 6335; E-mails: j.zhang@federation.edu.au; jiapu_zhang@hotmail.com

Background:

Molecular Dynamics (MD) studies of Buffalo Prion Protein (BufPrP^C) (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 BufPrP^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^C structure furthermore.

Results:

From the salt bridge point of view, we found an important reason why BufPrP^C 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 (PrP^C) to diseased infectious prions (PrP^Sc). 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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RESEARCH ARTICLE

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

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Abstract

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