DC pole | Wartość | Język |
dc.contributor.author | Bąk, Andrzej | - |
dc.contributor.author | Kozik, Violetta | - |
dc.contributor.author | Kozakiewicz, Dariusz | - |
dc.contributor.author | Gajcy, Kamila | - |
dc.contributor.author | Strub, Daniel Jan | - |
dc.contributor.author | Świetlicka, Aleksandra | - |
dc.contributor.author | Stepankova, Sarka | - |
dc.contributor.author | Imramovsky, Ales | - |
dc.contributor.author | Polański, Jarosław | - |
dc.contributor.author | Smoliński, Adam | - |
dc.contributor.author | Jampilek, Josef | - |
dc.date.accessioned | 2019-04-26T10:30:01Z | - |
dc.date.available | 2019-04-26T10:30:01Z | - |
dc.date.issued | 2019 | - |
dc.identifier.citation | International Journal of Molecular Sciences, Vol. 20, iss. 7 (2019), Art. No. | pl_PL |
dc.identifier.issn | 1422-0067 | - |
dc.identifier.uri | http://hdl.handle.net/20.500.12128/8991 | - |
dc.description.abstract | A series of new benzene-based derivatives was designed, synthesized and comprehensively
characterized. All of the tested compounds were evaluated for their in vitro ability to potentially
inhibit the acetyl- and butyrylcholinesterase enzymes. The selectivity index of individual molecules to
cholinesterases was also determined. Generally, the inhibitory potency was stronger against butyrylcompared
to acetylcholinesterase; however, some of the compounds showed a promising inhibition of
both enzymes. In fact, two compounds (23, benzyl ethyl(1-oxo-1-phenylpropan-2-yl)carbamate and 28,
benzyl (1-(3-chlorophenyl)-1-oxopropan-2-yl) (methyl)carbamate) had a very high selectivity index,
while the second one (28) reached the lowest inhibitory concentration IC50 value, which corresponds
quite well with galanthamine. Moreover, comparative receptor-independent and receptor-dependent
structure–activity studies were conducted to explain the observed variations in inhibiting the potential
of the investigated carbamate series. The principal objective of the ligand-based study was to
comparatively analyze the molecular surface to gain insight into the electronic and/or steric factors
that govern the ability to inhibit enzyme activities. The spatial distribution of potentially important
steric and electrostatic factors was determined using the probability-guided pharmacophore mapping
procedure, which is based on the iterative variable elimination method. Additionally, planar and
spatial maps of the host–target interactions were created for all of the active compounds and compared
with the drug molecules using the docking methodology. | pl_PL |
dc.language.iso | en | pl_PL |
dc.rights | Uznanie autorstwa 3.0 Polska | * |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/pl/ | * |
dc.subject | benzene-based carbamates | pl_PL |
dc.subject | in vitro cholinesterase inhibition | pl_PL |
dc.subject | CoMSA | pl_PL |
dc.subject | IVE-PLS | pl_PL |
dc.subject | molecular docking study | pl_PL |
dc.title | Novel Benzene-Based Carbamates for AChE/BChE Inhibition: Synthesis and Ligand/Structure-Oriented SAR Study | pl_PL |
dc.type | info:eu-repo/semantics/article | pl_PL |
dc.identifier.doi | 10.3390/ijms20071524 | - |
Pojawia się w kolekcji: | Artykuły (WNŚiT)
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