• Je něco špatně v tomto záznamu ?

Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane

H. Fatafta, M. Khaled, MC. Owen, A. Sayyed-Ahmad, B. Strodel

. 2021 ; 118 (39) : . [pub] 20210928

Jazyk angličtina Země Spojené státy americké

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc22003668
E-zdroje Online Plný text

NLK Free Medical Journals od 1915 do Před 6 měsíci
Freely Accessible Science Journals od 1915 do Před 6 měsíci
PubMed Central od 1915 do Před 6 měsíci
Europe PubMed Central od 1915 do Před 6 měsíci
Open Access Digital Library od 1915-01-15
Open Access Digital Library od 1915-01-01

Odkazy

PubMed 34544868
DOI 10.1073/pnas.2106210118
Knihovny.cz E-zdroje

Mounting evidence suggests that the neuronal cell membrane is the main site of oligomer-mediated neuronal toxicity of amyloid-β peptides in Alzheimer's disease. To gain a detailed understanding of the mutual interference of amyloid-β oligomers and the neuronal membrane, we carried out microseconds of all-atom molecular dynamics (MD) simulations on the dimerization of amyloid-β (Aβ)42 in the aqueous phase and in the presence of a lipid bilayer mimicking the in vivo composition of neuronal membranes. The dimerization in solution is characterized by a random coil to β-sheet transition that seems on pathway to amyloid aggregation, while the interactions with the neuronal membrane decrease the order of the Aβ42 dimer by attenuating its propensity to form a β-sheet structure. The main lipid interaction partners of Aβ42 are the surface-exposed sugar groups of the gangliosides GM1. As the neurotoxic activity of amyloid oligomers increases with oligomer order, these results suggest that GM1 is neuroprotective against Aβ-mediated toxicity.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc22003668
003      
CZ-PrNML
005      
20220127150009.0
007      
ta
008      
220113s2021 xxu f 000 0|eng||
009      
AR
024    7_
$a 10.1073/pnas.2106210118 $2 doi
035    __
$a (PubMed)34544868
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a xxu
100    1_
$a Fatafta, Hebah $u Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, 52425 Jülich, Germany
245    10
$a Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane / $c H. Fatafta, M. Khaled, MC. Owen, A. Sayyed-Ahmad, B. Strodel
520    9_
$a Mounting evidence suggests that the neuronal cell membrane is the main site of oligomer-mediated neuronal toxicity of amyloid-β peptides in Alzheimer's disease. To gain a detailed understanding of the mutual interference of amyloid-β oligomers and the neuronal membrane, we carried out microseconds of all-atom molecular dynamics (MD) simulations on the dimerization of amyloid-β (Aβ)42 in the aqueous phase and in the presence of a lipid bilayer mimicking the in vivo composition of neuronal membranes. The dimerization in solution is characterized by a random coil to β-sheet transition that seems on pathway to amyloid aggregation, while the interactions with the neuronal membrane decrease the order of the Aβ42 dimer by attenuating its propensity to form a β-sheet structure. The main lipid interaction partners of Aβ42 are the surface-exposed sugar groups of the gangliosides GM1. As the neurotoxic activity of amyloid oligomers increases with oligomer order, these results suggest that GM1 is neuroprotective against Aβ-mediated toxicity.
650    _2
$a amyloid $x chemie $7 D000682
650    _2
$a amyloidní beta-protein $x chemie $x metabolismus $7 D016229
650    _2
$a buněčná membrána $x metabolismus $7 D002462
650    _2
$a G(M1) gangliosid $x metabolismus $7 D005677
650    _2
$a lidé $7 D006801
650    _2
$a lipidové dvojvrstvy $x metabolismus $7 D008051
650    _2
$a simulace molekulární dynamiky $7 D056004
650    _2
$a neurony $x metabolismus $7 D009474
650    _2
$a vazba proteinů $7 D011485
650    _2
$a konformace proteinů $7 D011487
650    12
$a multimerizace proteinu $7 D055503
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Khaled, Mohammed $u Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, 52425 Jülich, Germany
700    1_
$a Owen, Michael C $u Central European Institute of Technology, Masaryk University, Brno 625 00, Czech Republic $u Institute of Chemistry, University of Miskolc, 3515 Miskolc-Egyetemváros, Hungary
700    1_
$a Sayyed-Ahmad, Abdallah $u Department of Physics, Birzeit University, 71939 Birzeit, Palestine
700    1_
$a Strodel, Birgit $u Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, 52425 Jülich, Germany; b.strodel@fz-juelich.de $u Institute of Theoretical and Computational Chemistry, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany
773    0_
$w MED00010472 $t Proceedings of the National Academy of Sciences of the United States of America $x 1091-6490 $g Roč. 118, č. 39 (2021)
856    41
$u https://pubmed.ncbi.nlm.nih.gov/34544868 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y p $z 0
990    __
$a 20220113 $b ABA008
991    __
$a 20220127150005 $b ABA008
999    __
$a ok $b bmc $g 1751201 $s 1154817
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2021 $b 118 $c 39 $e 20210928 $i 1091-6490 $m Proceedings of the National Academy of Sciences of the United States of America $n Proc Natl Acad Sci U S A $x MED00010472
LZP    __
$a Pubmed-20220113

Najít záznam

Citační ukazatele

Možnosti archivace