Open Access
Biophysical Journal, volume 102, issue 1, pages 136-143
NMR solution structure of rat Aβ(1-16): Toward understanding the mechanism of rats' resistance to Alzheimer's disease
Istrate Andrey N
1, 2, 3
,
Polshakov Vladimir I
,
Makarov Alexander A.
1, 2, 3
,
Козин С. А.
4, 5
,
Mantsyzov Alexey B.
1, 6, 7
,
Tsvetkov Philipp O
,
Tsvetkov Philipp O.
1, 2, 3
,
Kulikova Alexandra A
1, 2, 3
,
Polshakov Vladimir I.
1, 6, 7
1
Moscow Russia
|
2
RUSSIAN ACADEMY OF SCIENCES
5
7
Faculty of Fundamental Medicine
Publication type: Journal Article
Publication date: 2012-01-04
Journal:
Biophysical Journal
Quartile SCImago
Q1
Quartile WOS
Q2
Impact factor: 3.4
ISSN: 00063495, 15420086
PubMed ID:
22225807
Biophysics
Abstract
In an attempt to reveal the mechanism of rats' resistance to Alzheimer's disease, we determined the structure of the metal-binding domain 1-16 of rat β-amyloid (rat Aβ(1-16)) in solution in the absence and presence of zinc ions. A zinc-induced dimerization of the domain was detected. The zinc coordination site was found to involve residues His-6 and His-14 of both peptide chains. We used experimental restraints obtained from analyses of NMR and isothermal titration calorimetry data to perform structure calculations. The calculations employed an explicit water environment and a simulated annealing molecular-dynamics protocol followed by quantum-mechanical/molecular-mechanical optimization. We found that the C-tails of the two polypeptide chains of the rat Aβ(1-16) dimer are oriented in opposite directions to each other, which hinders the assembly of rat Aβ dimers into oligomeric aggregates. Thus, the differences in the structure of zinc-binding sites of human and rat Aβ(1-16), their ability to form regular cross-monomer bonds, and the orientation of their hydrophobic C-tails could be responsible for the resistance of rats to Alzheimer's disease.
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Istrate A. N. et al. NMR solution structure of rat Aβ(1-16): Toward understanding the mechanism of rats' resistance to Alzheimer's disease // Biophysical Journal. 2012. Vol. 102. No. 1. pp. 136-143.
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Istrate A. N., Tsvetkov P. O., Mantsyzov A. B., Kulikova A. A., Козин С. А., Makarov A. A., Polshakov V. I., Tsvetkov P. O., Kulikova A. A., Polshakov V. I. NMR solution structure of rat Aβ(1-16): Toward understanding the mechanism of rats' resistance to Alzheimer's disease // Biophysical Journal. 2012. Vol. 102. No. 1. pp. 136-143.
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TY - JOUR
DO - 10.1016/j.bpj.2011.11.4006
UR - https://doi.org/10.1016%2Fj.bpj.2011.11.4006
TI - NMR solution structure of rat Aβ(1-16): Toward understanding the mechanism of rats' resistance to Alzheimer's disease
T2 - Biophysical Journal
AU - Istrate, Andrey N
AU - Tsvetkov, Philipp O
AU - Mantsyzov, Alexey B.
AU - Kulikova, Alexandra A.
AU - Козин, С. А.
AU - Makarov, Alexander A.
AU - Polshakov, Vladimir I
AU - Tsvetkov, Philipp O.
AU - Kulikova, Alexandra A
AU - Polshakov, Vladimir I.
PY - 2012
DA - 2012/01/04 00:00:00
PB - Biophysical Society
SP - 136-143
IS - 1
VL - 102
PMID - 22225807
SN - 0006-3495
SN - 1542-0086
ER -
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@article{2012_Istrate,
author = {Andrey N Istrate and Philipp O Tsvetkov and Alexey B. Mantsyzov and Alexandra A. Kulikova and С. А. Козин and Alexander A. Makarov and Vladimir I Polshakov and Philipp O. Tsvetkov and Alexandra A Kulikova and Vladimir I. Polshakov},
title = {NMR solution structure of rat Aβ(1-16): Toward understanding the mechanism of rats' resistance to Alzheimer's disease},
journal = {Biophysical Journal},
year = {2012},
volume = {102},
publisher = {Biophysical Society},
month = {jan},
url = {https://doi.org/10.1016%2Fj.bpj.2011.11.4006},
number = {1},
pages = {136--143},
doi = {10.1016/j.bpj.2011.11.4006}
}
Cite this
MLA
Copy
Istrate, Andrey N., et al. “NMR solution structure of rat Aβ(1-16): Toward understanding the mechanism of rats' resistance to Alzheimer's disease.” Biophysical Journal, vol. 102, no. 1, Jan. 2012, pp. 136-143. https://doi.org/10.1016%2Fj.bpj.2011.11.4006.
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