Molecular dynamics study on the stability of wild-type and the R220K mutant of human prion protein

被引：8

作者：

Chen, Xin ^{[1
]}

Zhu, Shuyan ^{[1
]}

Wang, Shoubin ^{[1
]}

Yang, Dagang ^{[1
]}

Zhang, Jinglai ^{[1
]}

机构：

[1] Henan Univ, Inst Environm & Analyt Sci, Coll Chem & Chem Engn, Kaifeng 475001, Henan, Peoples R China

来源：

MOLECULAR SIMULATION | 2014年 / 40卷 / 06期

基金：

中国国家自然科学基金;

关键词：

stability; mutant; molecular dynamics simulation; hydrodynamics; human prion protein; GLYCOPROTEIN-IB; BETA-SWITCH; LOW PH; TEMPERATURE; SIMULATION; DISEASES; TRANSITION; VARIANTS; MUTATION; BIOLOGY;

D O I：

10.1080/08927022.2013.824572

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Prion diseases are invariably fatal and highly infectious neurodegenerative diseases related to the structure transition of -helix into -sheet. In order to gain more direct insight into the molecular basis of the disease, the stability of the wild-type human prion protein (hPrPc) and the R220K mutant (m-hPrPc) was studied by molecular dynamics (MD) and flow MD simulation. Both the thermodynamic stability and the mechanical properties of hPrPc were investigated in this work. It was found that -sheet was more readily to be unfolded in m-hPrPc. In the case of hPrPc, less content of helix was preserved after water turbulence. The H-bond network formed by the mutation-related residue 220 was found to play a key role in the stability of hPrPc.

引用

页码：504 / 513

页数：10

共 50 条

[41] The use of yeast mitochondria to study the properties of wild-type and mutant human mitochondrial ornithine transporter
Morizono, H
Woolston, JE
Colombini, M
Tuchman, M
MOLECULAR GENETICS AND METABOLISM, 2005, 86 (04) : 431 - 440
[42] K-Ras is required for maintaining survivin protein stability in human cancer cells harboring mutant but not wild type K-Ras
Tecleab, Awet
Sebti, Said M.
CANCER RESEARCH, 2011, 71
[43] Origins of the specificity of inhibitor P218 toward wild-type and mutant PfDHFR: a molecular dynamics analysis
Abbat, Sheenu
Jain, Vaibhav
Bharatam, Prasad V.
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 2015, 33 (09): : 1913 - 1928
[44] Stability of the β-structure in prion protein: A molecular dynamics study based on polarized force field
Xu, Zhijun
Lazim, Raudah
Mei, Ye
Zhang, Dawei
CHEMICAL PHYSICS LETTERS, 2012, 539 : 239 - 244
[45] Molecular dynamics study of membrane permeabilization by wild-type and mutant lytic peptides from the non-enveloped Flock House virus
Nangia, Shivangi
Boyd, Kevin J.
May, Eric R.
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2020, 1862 (02):
[46] Exploring the Inhibitory Efficacy of Resokaempferol and Tectochrysin on PI3Kα Protein by Combining DFT and Molecular Docking against Wild-Type and H1047R Mutant Forms
Paraschiv, Cristina
Gosav, Steluta
Burlacu, Catalina Mercedes
Praisler, Mirela
INVENTIONS, 2024, 9 (05)
[47] Investigating the Structure and Dynamics of the PIK3CA Wild-Type and H1047R Oncogenic Mutant
Gkeka, Paraskevi
Evangelidis, Thomas
Pavlaki, Maria
Lazani, Vasiliki
Christoforidis, Savvas
Agianian, Bogos
Cournia, Zoe
PLOS COMPUTATIONAL BIOLOGY, 2014, 10 (10)
[48] Structures of the E46K Mutant-Type α-Synuclein Protein and Impact of E46K Mutation on the Structures of the Wild-Type α-Synuclein Protein
Wise-Scira, Olivia
Dunn, Aquila
Aloglu, Ahmet K.
Sakallioglu, Isin T.
Coskuner, Orkid
ACS CHEMICAL NEUROSCIENCE, 2013, 4 (03): : 498 - 508
[49] Generating antibodies against the native form of the human prion protein (hPrP) in wild-type animals: A comparison between DNA and protein immunizations
Alexandrenne, Coralie
Wijkhuisen, Anne
Dkhissi, Fatima
Hanoux, Vincent
Creminon, Christophe
Boquet, Didier
Couraud, Jean-Yves
JOURNAL OF IMMUNOLOGICAL METHODS, 2009, 341 (1-2) : 41 - 49
[50] Discrimination of L- and D-chirality in oligoarginine peptides using the wild-type and R220s mutant aerolysin pores
Jain, Priyanka
Ensslen, Tobias
Behrends, Jan C.
BIOPHYSICAL JOURNAL, 2023, 122 (03) : 439A - 439A

← 1 2 3 4 5 →