(Z)-N-(3-([1,1'-biphenyl]-2-yl)-4-heptyl-4-hydroxythiazolidin-2-ylidene)-4-bromobenzamide as carbonic anhydrase inhibitor: exploration of its in vitro and in silico studies

BMC Chemistry, Journal Year: 2025, Volume and Issue: 19(1)

Published: March 10, 2025

Human Carbonic Anhydrase inhibitors (CAIs) have been clinically used to treat a variety of disorders, such as cancer, obesity, haemolytic anaemia, glaucoma, retinopathy, and epilepsy. To develop inhibitor, Iminothiazoline analogue ((Z)-N-(3-([1,1'-biphenyl]-2-yl)-4-heptyl-4-hydroxythiazolidin-2-ylidene)-4-bromobenzamide) was synthesized characterized. Single crystal X-Ray diffraction studies Hirshfeld surface analysis (HSA) were conducted find the exact molecular structure well intermolecular interactions. DFT Calculations indicated soft reactive nature molecule. In-Vitro carbonic anhydrase inhibition showed excellent potential (Z)-N-(3-([1,1'-biphenyl]-2-yl)-4-heptyl-4-hydroxythiazolidin-2-ylidene)-4-bromobenzamide (IC50 value 0.147 ± 0.03 µM). Four hydrogen bonds multiple hydrophobic interactions observed between molecule enzyme during Molecular docking studies. dynamic simulation that Protein–ligand complex generally remained stable throughout time. ADMET suggested need structural modification for drug like behavior

Language: Английский

Some Novel Oxirane-Thiirane Derivatives: Synthesis, Molecular docking and Enzymatic Inhibition for Therapeutic Potential

Cell Biochemistry and Biophysics, Journal Year: 2025, Volume and Issue: unknown

Published: April 7, 2025

Language: Английский

New Sulfonate Ester‐Linked Fluorinated Hydrazone Derivatives as Multitarget Carbonic Anhydrase and Cholinesterase Inhibitors: Design, Synthesis, Biological Evaluation, Molecular Docking and ADME Analysis

Chemistry & Biodiversity, Journal Year: 2024, Volume and Issue: 21(12)

Published: Aug. 19, 2024

Abstract In this study, some new hydrazone derivatives ( 2a – g ) was designed, synthesized for first time, and evaluated as multitarget inhibitors of AChE, BChE, hCA I II. The chemical structures hybrids were confirmed by elemental analysis spectroscopic techniques. All tested compounds showed low nanomolar inhibition with IC 50 values in the range 30.4–264.0 nM against I, 23.2–251.6 II, 12.1–114.3 76.4–134.0 BChE. These inhibited AChE more than acetazolamide (AZA) neostigmine. Among them, 2c 2e , which have a linear structure, determined to be most active inhibitor candidates these selected enzymes. Molecular docking studies carried out on 2a‐ ‐ ), revealing their binding interactions site II thus supporting experimental findings. Additionally, silico absorption, distribution, metabolism, excretion (ADME) prediction obtained approaches determine solubility, whether they potential cross blood‐brain barrier (BBB), such GI absorption drug likeness principles.

Language: Английский