Details
| Originalsprache | Englisch |
|---|---|
| Seitenumfang | 13 |
| Fachzeitschrift | Molecular diversity |
| Jahrgang | 25 |
| Ausgabenummer | 2 |
| Frühes Online-Datum | 24 Feb. 2020 |
| Publikationsstatus | Veröffentlicht - Mai 2021 |
Abstract
Abstract: Synthesis of a novel series of hydrazine clubbed 1,3-thiazoles (5a–m) has been described by reacting hydrazine-1-carbothioamides (3a–k) with α-chloro- or bromo-acetophenones (4a–d) in refluxing ethanol in good to excellent yields (65–86%). Structural confirmation was based upon spectroscopic techniques such as 1H-NMR, 13C-NMR, FT-IR and mass spectrometry. The biological application of these motifs has been demonstrated in terms of their strong urease inhibition activity. The results of in vitro study revealed that all the compounds are the potent inhibitors of urease. The IC 50 (ranging in between 110 and 440 nM) values were higher as compared to that of standard, i.e., thiourea (IC 50 = 490 ± 10 nM). The synthesized compounds were docked at the active sites of the Jack bean urease enzyme in order to explore the possible binding interactions of enzyme–ligand complexes; the results reinforced the in vitro biological activity results. Graphic abstract: [Figure not available: see fulltext.].
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- Pharmakologie, Toxikologie und Pharmazie (insg.)
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in: Molecular diversity, Jahrgang 25, Nr. 2, 05.2021.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Hydrazine clubbed 1,3-thiazoles as potent urease inhibitors: design, synthesis and molecular docking studies
AU - Channar, Pervaiz Ali
AU - Saeed, Aamer
AU - Afzal, Saira
AU - Hussain, Dilawar
AU - Kalesse, Markus
AU - Shehzadi, Syeda Aaliya
AU - Iqbal, Jamshed
N1 - Funding information: A.S. is grateful to Alexander von Humboldt Foundation Germany, for a Gerog Forster Post-doctoral fellowship. J.I. is thankful to the Higher Education Commission of Pakistan for the financial support through Project No. Ph-V-MG-3/Peridot/R&D/HEC/2019.
PY - 2021/5
Y1 - 2021/5
N2 - Abstract: Synthesis of a novel series of hydrazine clubbed 1,3-thiazoles (5a–m) has been described by reacting hydrazine-1-carbothioamides (3a–k) with α-chloro- or bromo-acetophenones (4a–d) in refluxing ethanol in good to excellent yields (65–86%). Structural confirmation was based upon spectroscopic techniques such as 1H-NMR, 13C-NMR, FT-IR and mass spectrometry. The biological application of these motifs has been demonstrated in terms of their strong urease inhibition activity. The results of in vitro study revealed that all the compounds are the potent inhibitors of urease. The IC 50 (ranging in between 110 and 440 nM) values were higher as compared to that of standard, i.e., thiourea (IC 50 = 490 ± 10 nM). The synthesized compounds were docked at the active sites of the Jack bean urease enzyme in order to explore the possible binding interactions of enzyme–ligand complexes; the results reinforced the in vitro biological activity results. Graphic abstract: [Figure not available: see fulltext.].
AB - Abstract: Synthesis of a novel series of hydrazine clubbed 1,3-thiazoles (5a–m) has been described by reacting hydrazine-1-carbothioamides (3a–k) with α-chloro- or bromo-acetophenones (4a–d) in refluxing ethanol in good to excellent yields (65–86%). Structural confirmation was based upon spectroscopic techniques such as 1H-NMR, 13C-NMR, FT-IR and mass spectrometry. The biological application of these motifs has been demonstrated in terms of their strong urease inhibition activity. The results of in vitro study revealed that all the compounds are the potent inhibitors of urease. The IC 50 (ranging in between 110 and 440 nM) values were higher as compared to that of standard, i.e., thiourea (IC 50 = 490 ± 10 nM). The synthesized compounds were docked at the active sites of the Jack bean urease enzyme in order to explore the possible binding interactions of enzyme–ligand complexes; the results reinforced the in vitro biological activity results. Graphic abstract: [Figure not available: see fulltext.].
KW - Hydrazine-1,3-thiazole
KW - Molecular docking
KW - Urease inhibition
UR - http://www.scopus.com/inward/record.url?scp=85106113720&partnerID=8YFLogxK
U2 - 10.1007/s11030-020-10057-7
DO - 10.1007/s11030-020-10057-7
M3 - Article
VL - 25
JO - Molecular diversity
JF - Molecular diversity
SN - 1381-1991
IS - 2
ER -