Molecular dynamics studies on the NMR structures of rabbit prion protein wild type and mutants: surface electrostatic charge distributions

被引:8
作者
Zhang, Jiapu [1 ,2 ,3 ]
Wang, Feng [1 ]
Zhang, Yuanli [4 ]
机构
[1] Swinburne Univ Technol, Mol Model Discovery Lab, Dept Chem & Biotechnol, Fac Sci Engn & Technol, Hawthorn, Vic 3122, Australia
[2] Federat Univ Australia, Grad Sch Sci Informat Technol & Engn, Fac Sci, Ballarat, Vic 3353, Australia
[3] Federat Univ Australia, Ctr Informat & Appl Optimisat, Fac Sci, Ballarat, Vic 3353, Australia
[4] Taishan Med Univ, Sch Basic Med Sci, Tai An 271000, Shandong, Peoples R China
关键词
NMR structures; surface electrostatic charge distributions; rabbit prion protein wild type and mutants; prion diseases; molecular dynamics study; SIMULATIONS; STABILITY; INFECTION; RESISTANT; RESIDUES; AMBER;
D O I
10.1080/07391102.2014.947325
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep and goats, cattle, deer and elk, and humans. But for rabbits, studies have shown that they have a low susceptibility to be infected by prion diseases. This paper does molecular dynamics (MD) studies of rabbit NMR structures (of the wild type and its two mutants of two surface residues), in order to understand the specific mechanism of rabbit prion proteins (RaPrPC). Protein surface electrostatic charge distributions are specially focused to analyze the MD trajectories. This paper can conclude that surface electrostatic charge distributions indeed contribute to the structural stability of wild-type RaPrPC; this may be useful for the medicinal treatment of prion diseases.
引用
收藏
页码:1326 / 1335
页数:10
相关论文
共 30 条
[1]   FATE OF ME7 SCRAPIE INFECTION IN RATS, GUINEA-PIGS AND RABBITS [J].
BARLOW, RM ;
RENNIE, JC .
RESEARCH IN VETERINARY SCIENCE, 1976, 21 (01) :110-111
[2]   Stabilizing Salt-Bridge Enhances Protein Thermostability by Reducing the Heat Capacity Change of Unfolding [J].
Chan, Chi-Ho ;
Yu, Tsz-Ha ;
Wong, Kam-Bo .
PLOS ONE, 2011, 6 (06)
[3]   Molecular Dynamics Simulations Capture the Misfolding of the Bovine Prion Protein at Acidic pH [J].
Cheng, Chin Jung ;
Daggett, Valerie .
BIOMOLECULES, 2014, 4 (01) :181-201
[4]   Rabbits are not resistant to prion infection [J].
Chianini, Francesca ;
Fernandez-Borges, Natalia ;
Vidal, Enric ;
Gibbard, Louise ;
Pintadoe, Belen ;
de Castro, Jorge ;
Priola, Suzette A. ;
Hamilton, Scott ;
Eaton, Samantha L. ;
Finlayson, Jeanie ;
Pang, Yvonne ;
Steele, Philip ;
Reid, Hugh W. ;
Dagleish, Mark P. ;
Castilla, Joaquin .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2012, 109 (13) :5080-5085
[5]   A cell line infectible by prion strains from different species [J].
Courageot, M. -P. ;
Daude, N. ;
Nonno, R. ;
Paquet, S. ;
Di Bari, M. A. ;
Le Dur, A. ;
Chapuis, J. ;
Hill, A. F. ;
Agrimi, U. ;
Laude, H. ;
Vilette, D. .
JOURNAL OF GENERAL VIROLOGY, 2008, 89 :341-347
[6]   Naturally prion resistant mammals A utopia? [J].
Fernandez-Borges, Natalia ;
Chianini, Francesca ;
Erana, Hasier ;
Vidal, Enric ;
Eaton, Samantha L. ;
Pintado, Belen ;
Finlayson, Jeanie ;
Dagleish, Mark P. ;
Castilla, Joaquin .
PRION, 2012, 6 (05)
[7]   In Vivo Generation of Neurotoxic Prion Protein: Role for Hsp70 in Accumulation of Misfolded Isoforms [J].
Fernandez-Funez, Pedro ;
Casas-Tinto, Sergio ;
Zhang, Yan ;
Gomez-Velazquez, Melisa ;
Morales-Garza, Marco A. ;
Cepeda-Nieto, Ana C. ;
Castilla, Joaquin ;
Soto, Claudio ;
Rincon-Limas, Diego E. .
PLOS GENETICS, 2009, 5 (06)
[8]   Routine Microsecond Molecular Dynamics Simulations with AMBER on GPUs. 1. Generalized Born [J].
Goetz, Andreas W. ;
Williamson, Mark J. ;
Xu, Dong ;
Poole, Duncan ;
Le Grand, Scott ;
Walker, Ross C. .
JOURNAL OF CHEMICAL THEORY AND COMPUTATION, 2012, 8 (05) :1542-1555
[9]   A theory for the anisotropic and inhomogeneous dielectric properties of proteins [J].
Guest, Will C. ;
Cashman, Neil R. ;
Plotkin, Steven S. .
PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 2011, 13 (13) :6286-6295
[10]  
Guest WC, 2010, BIOCHEM CELL BIOL, V88, P371, DOI [10.1139/O09-180, 10.1139/o09-180]