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    Design of novel benzimidazole-propane hydrazide derivatives as α-glucosidase and α-amylase inhibitors: in vitro and in silico studies
    (Springer Birkhauser, 2025) Mohammadizadeh, Shiva; Karimian, Somaye; Dastyafteh, Navid; Noori, Milad; Doraghi, Fatemeh; Mohammadi-Khanaposhtani, Maryam; Larijani, Bagher
    A new series of benzimidazole-propane hydrazide derivatives 9a-k were designed, synthesized, and evaluated for their inhibition ability against alpha-glucosidase and alpha-amylase. The results of the in vitro evaluations showed that all the tested compounds exhibited significant inhibition against alpha-glucosidase and alpha-amylase. Title compounds 9a-k exhibited varying degrees of inhibitory ability against alpha-glucosidase, with IC50 values in the range of 73.86-151.54 nM, in comparison to the standard acarbose drug with IC50 value of 174.50 nM. Similarly, these compounds demonstrated varying degrees of alpha-amylase inhibitory ability (the IC50 values ranged from 42.50 to 78.58 nM in comparison to acarbose with IC50 of 79.05 nM). Among the synthesized compounds, compound 9 h demonstrated the highest alpha-glucosidase inhibitory activity and compound 9 f demonstrated the highest anti-alpha-amylase activity. To further investigation on the potential of these derivatives as alpha-glucosidase and alpha-amylase inhibitors, molecular docking were conducted on all the synthesized compounds 9a-k. Docking results were in agreement with in vitro results. Molecular dynamics of compound 9 h showed that complex compound 9h-alpha-glucosidase had acceptable stability and flexibility. Calculations of physicochemical properties of compound 9a-k showed that these compounds fallowed of the main drug-likeness rules. Furthermore, the prediction of pharmacokinetics and toxicity profiles of compound 9 h showed that this compound can be considered as a lead drug structure.
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    Rhodanine-pyridinium derivatives as a new category of cholinesterase inhibitors: Design, synthesis, in vitro and in silico enzymatic evaluations
    (Elsevier, 2025) Noori, Milad; Karimian, Somaye; Dastyafteh, Navid; Ghafouri, Seyedeh Niloufar; Mohammadi-Khanaposhtani, Maryam; Safapoor, Sajedeh; Ghomi, Minoo Khalili
    Rhodanine-pyridinium derivatives 10a-q were designed and synthesized based on reported cholinesterase (ChE) inhibitors and evaluated as potent anti-Alzheimer's disease agents. The in vitro anti-ChE activity of the title compounds was evaluated against two main forms of this enzyme: acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). The obtained in vitro results showed that all the synthesized derivatives were more potent than positive control tacrine against AChE. Moreover, most of the new synthesized compounds were more potent than tacrine against BChE. Among the synthesized compounds, compound 10p was the most potent compound against AChE and compound 10f was the most potent compound against BChE. In vitro kinetic study demonstrated that compounds 10p and 10f were competitive inhibitors against AChE and BChE, respectively. Both these compounds had a 4-CF3 substituent on phenyl ring of benzyl pyridinium moiety. Docking study on compounds 10p and 10f demonstrated that these compounds with favorable binding energies in comparison to tacrine attached to the active sites of AChE and BChE. Molecular dynamics simulations were performed on the 10p-AChE and 10f-BChE complexes to gain deeper insights into the behavior of these compounds in the active sites of target enzymes.