TY - JOUR
T1 - Effects of lysine residues on structural characteristics and stability of tau proteins
AU - Lee, Myeongsang
AU - Baek, Inchul
AU - Choi, Hyunsung
AU - Kim, Jae In
AU - Na, Sungsoo
N1 - Funding Information:
S.N. gratefully acknowledges the Basic Science Research Program, through the National Research Foundation of Korea (NRF) and funded by the Ministry of Science, ICT & Future Planning (MSIP) (No. 2007–0056094 and No. 2014R1A2A1A11052389 ).
PY - 2015/10/23
Y1 - 2015/10/23
N2 - Pathological amyloid proteins have been implicated in neuro-degenerative diseases, specifically Alzheimer's, Parkinson's, Lewy-body diseases and prion related diseases. In prion related diseases, functional tau proteins can be transformed into pathological agents by environmental factors, including oxidative stress, inflammation, Aβ-mediated toxicity and covalent modification. These pathological agents are stable under physiological conditions and are not easily degraded. This un-degradable characteristic of tau proteins enables their utilization as functional materials to capturing the carbon dioxides. For the proper utilization of amyloid proteins as functional materials efficiently, a basic study regarding their structural characteristic is necessary. Here, we investigated the basic tau protein structure of wild-type (WT) and tau proteins with lysine residues mutation at glutamic residue (Q2K) on tau protein at atomistic scale. We also reported the size effect of both the WT and Q2K structures, which allowed us to identify the stability of those amyloid structures.
AB - Pathological amyloid proteins have been implicated in neuro-degenerative diseases, specifically Alzheimer's, Parkinson's, Lewy-body diseases and prion related diseases. In prion related diseases, functional tau proteins can be transformed into pathological agents by environmental factors, including oxidative stress, inflammation, Aβ-mediated toxicity and covalent modification. These pathological agents are stable under physiological conditions and are not easily degraded. This un-degradable characteristic of tau proteins enables their utilization as functional materials to capturing the carbon dioxides. For the proper utilization of amyloid proteins as functional materials efficiently, a basic study regarding their structural characteristic is necessary. Here, we investigated the basic tau protein structure of wild-type (WT) and tau proteins with lysine residues mutation at glutamic residue (Q2K) on tau protein at atomistic scale. We also reported the size effect of both the WT and Q2K structures, which allowed us to identify the stability of those amyloid structures.
KW - Amyloid proteins
KW - Lysine mutation
KW - Molecular dynamics
KW - Size effects
KW - Tau protein
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U2 - 10.1016/j.bbrc.2015.09.056
DO - 10.1016/j.bbrc.2015.09.056
M3 - Article
C2 - 26381172
AN - SCOPUS:84943352514
VL - 466
SP - 486
EP - 492
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -