Molecular Biology, volume 52, issue 4, pages 590-597
Enalaprilat Inhibits Zinc-Dependent Oligomerization of Metal-Binding Domain of Amyloid-beta Isoforms and Protects Human Neuroblastoma Cells from Toxic Action of these Isoforms
Kozin S A
1
,
Polshakov V I
2
,
Mezentsev Y V
3
,
Ivanov A. S.
3
,
Zhokhov S S
2
,
Yurinskaya M M
1, 4
,
Vinokurov M G
4
,
Makarov A. A.
1
,
Mitkevich V. A.
1
Publication type: Journal Article
Publication date: 2018-07-01
Journal:
Molecular Biology
Quartile SCImago
Q4
Quartile WOS
Q4
Impact factor: 1.2
ISSN: 00268933, 16083245
Structural Biology
Biophysics
Abstract
Intact amyloid-β peptides (Aβ) may undergo prion-like aggregation when they interact with chemically or structurally modified variants of Aβ present in extracellular pathohistological inclusions (amyloid plaques). This aggregation is regarded as one of the key molecular mechanisms of Alzheimer’s disease (AD) pathogenesis. Zinc ions are involved in the pathological dimerization and oligomerization of natural Aβ isoforms, and zinc-induced oligomers can also initiate the pathological aggregation of Aβ. Based on the earlier found molecular mechanism of zinc-dependent oligomerization of Aβ, it has been suggested that the targeted inhibition of the 11EVHH14 site in one Aβ molecule from zinc-mediated interactions with the same site of another Aβ molecule can effectively inhibit the oligomerization and aggregation of Aβ. Taking into account the similarity in the structural organization of zinc-binding sites within Aβ and angiotensin-converting enzyme (ACE), we hypothesized that inhibitors of the ACE active sites could specifically interact with the 11EVHH14 site of Aβ. Using a surface plasmon resonance biosensor and nuclear magnetic resonance spectroscopy, we have found that the ACE inhibitor enalaprilat effectively inhibits zinc-dependent dimerization of the metal-binding domains of intact Aβ and Aβ with isomerized Asp7 (isoAβ). We have also found that enalaprilat protects SH-SY5Y human neuroblastoma cells from the toxic effects of Aβ(1–42) and isoAβ(1–42), which are among the most common components of amyloid plaques. The results confirm the role of zincdependent oligomerization of Aβ in AD pathogenesis and make it possible one to consider enalaprilat as a prototype of antiaggregation agents for treating AD.
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Kozin S. A. et al. Enalaprilat Inhibits Zinc-Dependent Oligomerization of Metal-Binding Domain of Amyloid-beta Isoforms and Protects Human Neuroblastoma Cells from Toxic Action of these Isoforms // Molecular Biology. 2018. Vol. 52. No. 4. pp. 590-597.
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Kozin S. A., Polshakov V. I., Mezentsev Y. V., Ivanov A. S., Zhokhov S. S., Yurinskaya M. M., Vinokurov M. G., Makarov A. A., Mitkevich V. A. Enalaprilat Inhibits Zinc-Dependent Oligomerization of Metal-Binding Domain of Amyloid-beta Isoforms and Protects Human Neuroblastoma Cells from Toxic Action of these Isoforms // Molecular Biology. 2018. Vol. 52. No. 4. pp. 590-597.
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TY - JOUR
DO - 10.1134/S0026893318040106
UR - https://doi.org/10.1134%2FS0026893318040106
TI - Enalaprilat Inhibits Zinc-Dependent Oligomerization of Metal-Binding Domain of Amyloid-beta Isoforms and Protects Human Neuroblastoma Cells from Toxic Action of these Isoforms
T2 - Molecular Biology
AU - Kozin, S A
AU - Polshakov, V I
AU - Mezentsev, Y V
AU - Ivanov, A. S.
AU - Zhokhov, S S
AU - Yurinskaya, M M
AU - Vinokurov, M G
AU - Makarov, A. A.
AU - Mitkevich, V. A.
PY - 2018
DA - 2018/07/01 00:00:00
PB - Pleiades Publishing
SP - 590-597
IS - 4
VL - 52
SN - 0026-8933
SN - 1608-3245
ER -
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@article{2018_Kozin,
author = {S A Kozin and V I Polshakov and Y V Mezentsev and A. S. Ivanov and S S Zhokhov and M M Yurinskaya and M G Vinokurov and A. A. Makarov and V. A. Mitkevich},
title = {Enalaprilat Inhibits Zinc-Dependent Oligomerization of Metal-Binding Domain of Amyloid-beta Isoforms and Protects Human Neuroblastoma Cells from Toxic Action of these Isoforms},
journal = {Molecular Biology},
year = {2018},
volume = {52},
publisher = {Pleiades Publishing},
month = {jul},
url = {https://doi.org/10.1134%2FS0026893318040106},
number = {4},
pages = {590--597},
doi = {10.1134/S0026893318040106}
}
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Kozin, S. A., et al. “Enalaprilat Inhibits Zinc-Dependent Oligomerization of Metal-Binding Domain of Amyloid-beta Isoforms and Protects Human Neuroblastoma Cells from Toxic Action of these Isoforms.” Molecular Biology, vol. 52, no. 4, Jul. 2018, pp. 590-597. https://doi.org/10.1134%2FS0026893318040106.
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