Design, Synthesis,  &lt;i&gt;in vitro&lt;/i&gt; Enzymatic Evaluations, Molecular Modeling, Molecular Dynamics, and ADMET Prediction of Thieno[2,3-B]Quinoline-Hydrazones as Novel Inhibitors for α-Glucosidase

Noori, Milad; Rastak, Mryam; Halimi, Mohammad; Ghomi, Minoo Khalili; Mollazadeh, Mrjan; Mohammadi‐Khanaposhtani, Maryam; Sayahi, Mohammad Hosein; Mojtabavi, Somayeh; Faramarzi, Mohammad Ali; Larijani, Bagher; Biglar, Mahmoud; Amanlou, Massoud; Mahdavi, Mohammad

doi:10.2139/ssrn.4078391

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Unclassified

Year Published

2023

Publication Types

Select...

Article1

Relationship

Self Cite0

Independent1

Authors

Journals

Cited by 1 publication

(1 citation statement)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…www.nature.com/scientificreports/ effects such as abdominal distention, bloating, and diarrhea 8,9 . Thus, the discovery of new, abundant, and safe α-glucosidase inhibitors is highly needed 10 .…”

unclassified

Synthesis, in vitro α-glucosidase inhibitory activities, and molecular dynamic simulations of novel 4-hydroxyquinolinone-hydrazones as potential antidiabetic agents

Shayegan

Haghipour

Tanideh

et al. 2023

Sci Rep

View full text Add to dashboard Cite

In the present study, new structural variants of 4-hydroxyquinolinone-hydrazones were designed and synthesized. The structure elucidation of the synthetic derivatives 6a–o was carried out using different spectroscopic techniques including FTIR, 1H-NMR, 13C-NMR, and elemental analysis, and their α-glucosidase inhibitory activity was also determined. The synthetic molecules 6a–o exhibited good α-glucosidase inhibition with IC50 values ranging between 93.5 ± 0.6 to 575.6 ± 0.4 µM as compared to the standard acarbose (IC50 = 752.0 ± 2.0 µM). Structure–activity relationships of this series were established which is mainly based on the position and nature of the substituent on the benzylidene ring. A kinetic study of the active compounds 6l and 6m as the most potent derivatives were also carried out to confirm the mode of inhibition. The binding interactions of the most active compounds within the active site of the enzyme were determined by molecular docking and molecular dynamic simulations.

show abstract

unclassified