Michalina Hebda (Author),
Marek Bajda (Author),
Anna Więckowska (Author),
Natalia Szałaj (Author),
Anna Pasieka (Author),
Dawid Panek (Author),
Justyna Godyń (Author),
Tomasz Wichur (Author),
Damijan Knez (Author),
Stanislav Gobec (Author),
Barbara Malawska (Author)
Abstract
Cholinesterases and amyloid beta are one of the major biological targets in the search for a new and efficacious treatment of Alzheimer's disease. The study describes synthesis and pharmacological evaluation of new compounds designed as dual binding site acetylcholinesterase inhibitors. Among the synthesized compounds, two deserve special attention compounds 42 and 13. The former is a saccharin derivative and the most potent and selective acetylcholinesterase inhibitor (EeAChE IC50 = 70 nM). Isoindoline-1,3-dione derivative 13 displays balanced inhibitory potency against acetyl- and butyrylcholinesterase (BuChE) (EeAChE IC50 = 0.76 microM, EqBuChE IC50 = 0.618 microM), and it inhibits amyloid beta aggregation (35.8% at 10 microM). Kinetic studies show that the developed compounds act as mixed or non-competitive acetylcholinesterase inhibitors. According to molecular modelling studies, they are able to interact with both catalytic and peripheral active sites of the acetylcholinesterase. Their ability to cross the blood-brain barrier (BBB) was confirmed in vitro in the parallel artificial membrane permeability BBB assay. These compounds can be used as a solid starting point for further development of novel multifunctional ligands as potential anti-Alzheimer's agents.
Keywords
tarčna zdravila;razvoj zdravil;zaviralci acetilholinesteraze;molekularno modeliranje;
Data
Language: |
English |
Year of publishing: |
2016 |
Typology: |
1.01 - Original Scientific Article |
Organization: |
UL FFA - Faculty of Pharmacy |
UDC: |
615.2:616.894 |
COBISS: |
4051313
|
ISSN: |
1420-3049 |
Views: |
191 |
Downloads: |
61 |
Average score: |
0 (0 votes) |
Metadata: |
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Other data
Secondary language: |
Slovenian |
Secondary keywords: |
Alzheimerjeva bolezen; |
Type (COBISS): |
Article |
Pages: |
str. 1-24 |
Volume: |
ǂVol. ǂ21 |
Issue: |
ǂiss. ǂ4 |
Chronology: |
2016 |
DOI: |
10.3390/molecules21040410 |
ID: |
13390856 |