Computational studies of acetylcholinesterase complexed with fullerene derivatives: a new insight for Alzheimer disease treatment
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18450%2F16%3A50004681" target="_blank" >RIV/62690094:18450/16:50004681 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1080/07391102.2015.1077345" target="_blank" >http://dx.doi.org/10.1080/07391102.2015.1077345</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1080/07391102.2015.1077345" target="_blank" >10.1080/07391102.2015.1077345</a>
Alternative languages
Result language
angličtina
Original language name
Computational studies of acetylcholinesterase complexed with fullerene derivatives: a new insight for Alzheimer disease treatment
Original language description
Here, we propose five fullerene (C60) derivatives as new drugs against Alzheimer's disease (AD). These compounds were designed to act as new human acetylcholinesterase (HssAChE) inhibitors by blocking its fasciculin II (FASII) binding site. Docking and molecular dynamic results show that our proposals bind to the HssAChE tunnel entrance, forming stable complex, and further binding free energy calculations suggest that three of the derivatives proposed here could be potent HssAChE inhibitors. We found a region formed by a set of residues (Tyr72, Asp74, Trp286, Gln291, Tyr341, and Pro344) which can be further exploited in the drug design of new inhibitors of HssAChE based on C60 derivatives. Results presented here report for the first time by a new class of molecules that can become effective drugs against AD.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10406 - Analytical chemistry
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of biomolecular structure and dynamics
ISSN
0739-1102
e-ISSN
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Volume of the periodical
34
Issue of the periodical within the volume
6
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
1307-1316
UT code for WoS article
000375330300014
EID of the result in the Scopus database
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