Role of Oxidized Gly25, Gly29, and Gly33 Residues on the
Interactions of A beta(1-42) with Lipid Membranes

J 2020

Role of Oxidized Gly25, Gly29, and Gly33 Residues on the Interactions of A beta(1-42) with Lipid Membranes

FATAFTA, H., C. POOJARI, A. SAYYED-AHMAD, B. STRODEL, Michael Christopher OWEN et. al.

Základní údaje

Originální název

Role of Oxidized Gly25, Gly29, and Gly33 Residues on the Interactions of A beta(1-42) with Lipid Membranes

Autoři

FATAFTA, H., C. POOJARI, A. SAYYED-AHMAD, B. STRODEL a Michael Christopher OWEN (124 Kanada, garant, domácí)

Vydání

ACS CHEMICAL NEUROSCIENCE, WASHINGTON, AMER CHEMICAL SOC, 2020, 1948-7193

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.418

Kód RIV

RIV/00216224:14740/20:00118347

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1021/acschemneuro.9b00558

UT WoS

000515195800005

Klíčová slova anglicky

Amyloid-beta peptide; molecular dynamics; membrane simulations; oxidative stress; GM1; peptide membrane interactions

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 8. 3. 2021 20:36, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

Oxidative stress is known to play an important role in the pathogenesis of Alzheimer's disease. Moreover, it is becoming increasingly evident that the plasma membrane of neurons plays a role in modulating the aggregation and toxicity of Alzheimer's amyloid-beta peptide (A beta). In this study, the combined and interdependent effects of oxidation and membrane interactions on the 42 residues long A beta isoform are investigated using molecular simulations. Hamiltonian replica exchange molecular dynamics simulations are utilized to elucidate the impact of selected oxidized glycine residues of A beta 42 on the interactions of the peptide with a model membrane comprised of 70% POPC, 25% cholesterol, and 5% of the ganglioside GM1. The main findings are that, independent of the oxidation state, A beta prefers binding to GM1 over POPC, which is further enhanced by the oxidation of Gly29 and Gly33 and reduced the formation of beta-sheet. Our results suggest that the differences observed in A beta 42 conformations and its interaction with a lipid bilayer upon oxidation originate from the position of the oxidized Gly residue with respect to the hydrophobic sequence of A beta 42 involving the Gly29-XXX-Gly33-XXX-Gly37 motif and from specific interactions between the peptide and the terminal sugar groups of GM1.

Citovat

FATAFTA, H., C. POOJARI, A. SAYYED-AHMAD, B. STRODEL a Michael Christopher OWEN. Role of Oxidized Gly25, Gly29, and Gly33 Residues on the Interactions of A beta(1-42) with Lipid Membranes. ACS CHEMICAL NEUROSCIENCE. WASHINGTON: AMER CHEMICAL SOC, 2020, roč. 11, č. 4, s. 535-548, 27 s. ISSN 1948-7193. Dostupné z: https://dx.doi.org/10.1021/acschemneuro.9b00558.

@article{1750456,
   author = {Fatafta, H. and Poojari, C. and SayyedandAhmad, A. and Strodel, B. and Owen, Michael Christopher},
   article_location = {WASHINGTON},
   article_number = {4},
   doi = {http://dx.doi.org/10.1021/acschemneuro.9b00558},
   keywords = {Amyloid-beta peptide; molecular dynamics; membrane simulations; oxidative stress; GM1; peptide membrane interactions},
   language = {eng},
   issn = {1948-7193},
   journal = {ACS CHEMICAL NEUROSCIENCE},
   title = {Role of Oxidized Gly25, Gly29, and Gly33 Residues on the Interactions of A beta(1-42) with Lipid Membranes},
   url = {https://pubs.acs.org/doi/10.1021/acschemneuro.9b00558},
   volume = {11},
   year = {2020}
}

TY  - JOUR
ID  - 1750456
AU  - Fatafta, H. - Poojari, C. - Sayyed-Ahmad, A. - Strodel, B. - Owen, Michael Christopher
PY  - 2020
TI  - Role of Oxidized Gly25, Gly29, and Gly33 Residues on the Interactions of A beta(1-42) with Lipid Membranes
JF  - ACS CHEMICAL NEUROSCIENCE
VL  - 11
IS  - 4
SP  - 535-548
EP  - 535-548
PB  - AMER CHEMICAL SOC
SN  - 19487193
KW  - Amyloid-beta peptide
KW  - molecular dynamics
KW  - membrane simulations
KW  - oxidative stress
KW  - GM1
KW  - peptide membrane interactions
UR  - https://pubs.acs.org/doi/10.1021/acschemneuro.9b00558
N2  - Oxidative stress is known to play an important role in the pathogenesis of Alzheimer's disease. Moreover, it is becoming increasingly evident that the plasma membrane of neurons plays a role in modulating the aggregation and toxicity of Alzheimer's amyloid-beta peptide (A beta). In this study, the combined and interdependent effects of oxidation and membrane interactions on the 42 residues long A beta isoform are investigated using molecular simulations. Hamiltonian replica exchange molecular dynamics simulations are utilized to elucidate the impact of selected oxidized glycine residues of A beta 42 on the interactions of the peptide with a model membrane comprised of 70% POPC, 25% cholesterol, and 5% of the ganglioside GM1. The main findings are that, independent of the oxidation state, A beta prefers binding to GM1 over POPC, which is further enhanced by the oxidation of Gly29 and Gly33 and reduced the formation of beta-sheet. Our results suggest that the differences observed in A beta 42 conformations and its interaction with a lipid bilayer upon oxidation originate from the position of the oxidized Gly residue with respect to the hydrophobic sequence of A beta 42 involving the Gly29-XXX-Gly33-XXX-Gly37 motif and from specific interactions between the peptide and the terminal sugar groups of GM1.
ER  -

FATAFTA, H., C. POOJARI, A. SAYYED-AHMAD, B. STRODEL a Michael Christopher OWEN. Role of Oxidized Gly25, Gly29, and Gly33 Residues on the Interactions of A beta(1-42) with Lipid Membranes. \textit{ACS CHEMICAL NEUROSCIENCE}. WASHINGTON: AMER CHEMICAL SOC, 2020, roč.~11, č.~4, s.~535-548, 27 s. ISSN~1948-7193. Dostupné z: https://dx.doi.org/10.1021/acschemneuro.9b00558.

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