This research reports
the synthesis of new benzimidazole-derived
N
-acylhydrazones
(NAH), their characterization using various
spectroscopic methods, and in vitro evaluation as potent carbonic
anhydrase-II inhibitors. Among the target compounds (
9–29
), few showed higher inhibition than the standard acetazolamide (IC
50
: 18.6 ± 0.43 μM), for example, compound
9
(IC
50
: 13.3 ± 1.25 μM),
10
(IC
50
: 17.2 ± 1.24 μM),
12
(IC
50
: 14.6 ± 0.62 μM), and
15
(IC
50
: 14.5 ± 1.05 μM). Molecular docking was performed
on the most active compounds, which revealed their binding interactions
with the active site of the enzyme, thus supporting the experimental
findings.
A series of new heterocycles (4–18) was synthesized by the structural modification of benzimidazole‐2‐thiol (BT, 2‐MBI). The structures of the synthesized compounds were confirmed with the help of high‐resolution mass spectrometry (HRMS) and 1HNMR spectroscopy. High inhibitions of the oxidants such as ABTS and DPPH were observed for compounds 9 [IC50(s) = 167.4 μM (ABTS), 139.5 μM (DPPH)], 10 [IC50(s) = 186.5 μM (ABTS), 155.4 μM (DPPH)], 11 [IC50(s) = 286.1 μM (ABTS), 189.1 μM (DPPH)], 12 [IC50(s) = 310.8 μM (ABTS), 162.2 μM (DPPH)], 14 [IC50(s) = 281.3 μM (ABTS), 205.7 μM (DPPH)], 15 [IC50(s) = 284.1 μM (ABTS), 177.3 μM (DPPH)], and 16 [IC50(s) = 344.7 μM (ABTS), 270.2 μM (DPPH)] as compared with Ascorbic acid [IC50(s) = 340.9 μM (ABTS), 164.3 μM (DPPH)]. The anti‐Alzheimer's activity was performed in vitro against cholinesterase enzymes (AChE, BChE). Compound 11 was able to show significant inhibitions [IC50(s) = 121.2 μM (AChE), 38.3 μM (BChE)] as against that of galantamine [IC50(s) = 139.4 μM (AChE), 40.3 μM (BChE)]. Compound 14 was found as a very good inhibitor of butyrylcholinesterase (IC50 = 35.4 μM) as compared with standard galantamine. Molecular docking was further performed to investigate the mechanism of anticholinesterase activity.
A novel series of multifunctional benzimidazoles has been reported as potent inhibitors of α-glucosidase. The procedure relies on the synthesis of 5-amino-1H-benzo[d]imidazole-2-thiol 5 via the multistep reaction through 2-nitroaniline 1, benzene-1,2-diamine 2, 1H-benzo[d]imidazole-2-thiol 3, and 5-nitro-1H-benzo[d]imidazole-2-thiol 4. Further treatment of 5 with aromatic aldehydes 6a−m provided access to the target 5-(arylideneamino)-1H-benzo[d]imidazole-2-thiols 7a−m.The results of the bioactivity assessment revealed all the compounds as excellent inhibitors of the enzyme (IC 50 range: 0.64 ± 0.05 μM to 343.10 ± 1.62 μM) than acarbose (873.34 ± 1.21). Among them, 7i was the most active inhibitor (IC 50 : 0.64 ± 0.05 μM) followed by 7d
In the current study, a series of stabilized bis-acetylene incorporated 4-hydroxybenzaldehyde based macrocycles using the alkyne-homocoupling approach were synthesized in moderate yields. A total of six newly stiff macrocycles were synthesized in a stepwise manner starting from 4-hydroxybenzaldehyde. In the first step, base mediated propargylation was performed followed by copper mediated terminal alkyne homocoupling. The alkyne homocoupled substrate having carbonyl at both the terminals is cyclized in the final step via double imine formation reactions using substituted diamines as linker. All the newly synthesized rigid framework of the macrocycles were optimized at B3LYP/6-31G (d,p) level of theory. Nonlinear optical behaviors of the synthesized macrocycles were explored by the DFT calculations where high values of first-order hyperpolarizability and dipole moment were examined. In the reported study, a good agreement between experimental and theoretical parameters was observed that may play a significant contribution for the NLO applications.
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