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| Home > Publications database > All - d - Enantiomeric Peptide D3 Designed for Alzheimer’s Disease Treatment Dynamically Interacts with Membrane-Bound Amyloid-β Precursors > print |
| Home > Publications database > All - d - Enantiomeric Peptide D3 Designed for Alzheimer’s Disease Treatment Dynamically Interacts with Membrane-Bound Amyloid-β Precursors > print |
| 001 | 905388 | ||
| 005 | 20220318173147.0 | ||
| 024 | 7 | _ | |a 10.1021/acs.jmedchem.1c00632 |2 doi |
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| 100 | 1 | _ | |a Bocharov, Eduard V. |0 0000-0002-3635-1609 |b 0 |
| 245 | _ | _ | |a All - d - Enantiomeric Peptide D3 Designed for Alzheimer’s Disease Treatment Dynamically Interacts with Membrane-Bound Amyloid-β Precursors |
| 260 | _ | _ | |a Washington, DC |c 2021 |b ACS |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1642441047_30509 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 500 | _ | _ | |a Kein Post-print vorhanden |
| 520 | _ | _ | |a Alzheimer’s disease (AD) is a severe neurodegenerative pathology with no effective treatment known. Toxic amyloid-β peptide (Aβ) oligomers play a crucial role in AD pathogenesis. All-d-Enantiomeric peptide D3 and its derivatives were developed to disassemble and destroy cytotoxic Aβ aggregates. One of the D3-like compounds is approaching phase II clinical trials; however, high-resolution details of its disease-preventing or pharmacological actions are not completely clear. We demonstrate that peptide D3 stabilizing Aβ monomer dynamically interacts with the extracellular juxtamembrane region of a membrane-bound fragment of an amyloid precursor protein containing the Aβ sequence. MD simulations based on NMR measurement results suggest that D3 targets the amyloidogenic region, not compromising its α-helicity and preventing intermolecular hydrogen bonding, thus creating prerequisites for inhibition of early steps of Aβ conversion into β-conformation and its toxic oligomerization. An enhanced understanding of the D3 action molecular mechanism facilitates development of effective AD treatment and prevention strategies. |
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| 700 | 1 | _ | |a Gremer, Lothar |0 P:(DE-Juel1)145165 |b 1 |
| 700 | 1 | _ | |a Urban, Anatoly S. |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Okhrimenko, Ivan S. |0 0000-0002-1053-2778 |b 3 |
| 700 | 1 | _ | |a Volynsky, Pavel E. |0 P:(DE-HGF)0 |b 4 |
| 700 | 1 | _ | |a Nadezhdin, Kirill D. |0 P:(DE-HGF)0 |b 5 |
| 700 | 1 | _ | |a Bocharova, Olga V. |0 P:(DE-HGF)0 |b 6 |
| 700 | 1 | _ | |a Kornilov, Daniil A. |0 P:(DE-HGF)0 |b 7 |
| 700 | 1 | _ | |a Zagryadskaya, Yuliya A. |0 P:(DE-HGF)0 |b 8 |
| 700 | 1 | _ | |a Kamynina, Anna V. |0 P:(DE-HGF)0 |b 9 |
| 700 | 1 | _ | |a Kuzmichev, Pavel K. |0 0000-0001-5322-3580 |b 10 |
| 700 | 1 | _ | |a Kutzsche, Janine |0 P:(DE-Juel1)159137 |b 11 |u fzj |
| 700 | 1 | _ | |a Bolakhrif, Najoua |0 P:(DE-Juel1)180739 |b 12 |u fzj |
| 700 | 1 | _ | |a Müller-Schiffmann, Andreas |0 P:(DE-HGF)0 |b 13 |
| 700 | 1 | _ | |a Dencher, Norbert A. |0 P:(DE-HGF)0 |b 14 |
| 700 | 1 | _ | |a Arseniev, Alexander S. |0 P:(DE-HGF)0 |b 15 |
| 700 | 1 | _ | |a Efremov, Roman G. |0 0000-0002-5474-4721 |b 16 |
| 700 | 1 | _ | |a Gordeliy, Valentin I. |0 P:(DE-Juel1)131964 |b 17 |e Corresponding author |
| 700 | 1 | _ | |a Willbold, Dieter |0 P:(DE-Juel1)132029 |b 18 |e Corresponding author |
| 773 | _ | _ | |a 10.1021/acs.jmedchem.1c00632 |g Vol. 64, no. 22, p. 16464 - 16479 |0 PERI:(DE-600)1491411-6 |n 22 |p 16464 - 16479 |t Journal of medicinal chemistry |v 64 |y 2021 |x 0022-2623 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/905388/files/acs.jmedchem.1c00632.pdf |y Restricted |
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