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Novel Sulfonamide-Based Carbamates as Selective Inhibitors of BChE

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216275%3A25310%2F21%3A39917742" target="_blank" >RIV/00216275:25310/21:39917742 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.mdpi.com/1422-0067/22/17/9447" target="_blank" >https://www.mdpi.com/1422-0067/22/17/9447</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/ijms22179447" target="_blank" >10.3390/ijms22179447</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Novel Sulfonamide-Based Carbamates as Selective Inhibitors of BChE

  • Original language description

    A series of 14 target benzyl [2-(arylsulfamoyl)-1-substituted-ethyl]carbamates was prepared by multi-step synthesis and characterized. All the final compounds were tested for their ability to inhibit acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) in vitro, and the selectivity index (SI) was determined. Except for three compounds, all compounds showed strong preferential inhibition of BChE, and nine compounds were even more active than the clinically used rivastigmine. Benzyl {(2S)-1-[(2-methoxybenzyl)sulfamoyl]-4-methylpentan-2-yl}carbamate, benzyl {(2S)-1-[(4-chlorobenzyl)sulfamoyl]-4-methylpentan-2-yl}carbamate, and benzyl [(2S)-1-(benzylsulfamoyl)-4-methylpentan-2-yl]carbamate showed the highest BChE inhibition (IC50 = 4.33, 6.57, and 8.52 mu M, respectively), indicating that the last two derivatives had approximately 5-fold higher inhibitory activity against BChE than rivastigmine, and the first one was even 9-fold more effective than rivastigmine. In addition, the selectivity index was approx. 10 or 34, respectively. The process of carbamylation and reactivation of BChE was studied for the most active derivatives 5k, 5j. The detailed information about the mode of binding of these compounds to the active site of both BChE and AChE was obtained in a molecular modeling study. In this study, combined techniques (docking, molecular dynamic simulations, and QTAIM (quantum theory of atoms in molecules) calculations) were employed.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10401 - Organic chemistry

Result continuities

  • Project

    <a href="/en/project/GA18-03847S" target="_blank" >GA18-03847S: Pseudopeptide proteasome inhibitors</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2021

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    International Journal of Molecular Sciences

  • ISSN

    1661-6596

  • e-ISSN

  • Volume of the periodical

    22

  • Issue of the periodical within the volume

    17

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    30

  • Pages from-to

    9447

  • UT code for WoS article

    000694302900001

  • EID of the result in the Scopus database

    2-s2.0-85114049409