Investigation of inhibitory properties of some hydrazone compounds on hCA I, hCA II and AChE enzymes

Küçükoğlu, Kaan; Gül, Halise İnci; Taslimi, Parham; Gülçın, İlhami; Supuran, Claudiu T.

doi:10.1016/j.bioorg.2019.02.008

Cited by 130 publications

(36 citation statements)

References 78 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Comparing current results with previous results, it was found that novel bromophenols (Ki: 159.6-924.2 nM) [4] , oxazolidinone (Ki: 16.5-35.6 nM) [48] , pyrazolines (Ki: 48.2-84.1 nM) [76] , hydrazones (Ki: 66-128 nM) [77] , tacrine derivatives (Ki: 68-8480 nM) [78] , sulfamides (Ki: 0.027-0.076 nM) [79] , olivetol (Ki: 3.40 nM) [73] , and benzenesulfonamides (Ki: 22.7-109.1 nM) [80] effectively inhibited AChE enzyme. As seen in Figure 4, α-glycosidase enzyme, which released from intestine cells, hydrolyzes the oligosaccharides and polysaccharide to monosaccharide units, such as glucose and fructose in small intestine.…”

Section: Resultssupporting

confidence: 78%

The inhibition profile of sesamol against α-glycosidase and acetylcholinesterase enzymes

Topal

2019

International Journal of Food Properties

View full text Add to dashboard Cite

Sesamol (1,3-benzodioxol-5-ol) is found in the oilseed product, sesame. In our study, the inhibitory effects of sesamol compound on acetylcholinesterase and α-glycosidase enzymes were evaluated. Another aim of this study was to compare the inhibitory effects of sesamol to acarbose for α-glycosidase enzyme and tacrine for acetylcholinesterase (AChE). Sesamol exhibited noncompetitive inhibition for both metabolic enzymes. IC 50 values for AChE and αglycosidase enzymes were calculated as 86.63 nM and 99.00 nM, respectively. On the other hand, K i values were calculated as 46.68 nM and 75.33 nM for AChE and α-glycosidase enzymes, respectively. According to the obtained results showed effective inhibition at low concentrations. ARTICLE HISTORY

show abstract

Section: Resultssupporting

confidence: 78%

The inhibition profile of sesamol against α-glycosidase and acetylcholinesterase enzymes

Topal

2019

International Journal of Food Properties

View full text Add to dashboard Cite

show abstract

“…These reasons suggest that, knowing the inhibition mechanism of CA enzyme and synthesizing new inhibitory compounds have gained great importance. [ 55 ] Lately, the interactions of these two isoenzymes with melatonin, rosmarinic acid, dantrolene, taxifolin, morphine, capsaicin, vitamin E, ethanol, guaiacol and catechol, a series of antioxidant phenols, caffeic acid phenethyl ester, phenolic acids, benzotropones, sulfamides, acylsulfonamides, polyphenols and phenolic acids, bromophenols, dopaminergic compounds, sulfonamides, benzenesulfonamides, benzylsulfamides, carbamates and sulfamoylcarbamates, symmetric sulfamides, isatin Mannich bases, 𝛽‐lactam, carbamates, spirobisnaphthalenes, dimethoxy‐bromophenol, dimethoxybenzenes, trimethoxyindane, benzylamines, benzylsulfamides, trimethoxyindanes, avermectins, and hydroquinone have been studied. [ 56 ] Inhibition of some metabolic enzymes was investigated, and their results were reported as follows.…”

Section: Resultsmentioning

confidence: 99%

Supramolecular complexes of Ni (II) and Co (II) 4‐aminobenzoate with 3‐cyanopyridine: Synthesis, spectroscopic characterization, crystal structure, and enzyme inhibitory properties

Sertçelik

Öztürkkan

Taslimi

et al. 2021

Applied Organom Chemis

Self Cite

View full text Add to dashboard Cite

Two new complexes, [M (AB)2(CP)2(H2O)2] (where M = Ni and Co AB = 4‐aminobenzoate and CP = cyanopyridine), were synthesized and characterized using different techniques (elemental analysis, FT‐IR spectrophotometer, LC/MS, single‐crystal X‐ray diffraction, and TGA/DTA analysis). As a result of X‐ray structural analysis, it was determined that complexes are isostructural. In the crystalline structures, MII ions are bridged with their carboxylate oxygen and aminopyridine nitrogen atoms and their symmetry‐related counterparts to form a two‐dimensional polymeric structure. The MII ion is octa‐coordinated with two nitrogen atoms and two oxygen atoms of the AB and two atoms of the CP anions. In this study, the effect of these molecules, containing a biologically active group, was investigated on important metabolic enzymes (carbonic anhydrase isoenzymes I and II (hCA I and II), achethylcholinesterase (AChE), and α‐glycosidase (α‐Gly) enzymes).

show abstract

“…[ 3,10,46–49 ] AChE and BChE inhibitory effects of triazene‐substituted sulfamerazine derivatives ( 1 – 9 ) were measured by Ellman's method, [ 50 ] as described previously. [ 46,47,51 ] Acetylthiocholine iodide (AChI) and butyrylthiocholine iodide (BChI) were used as substrates for both enzymatic reactions. Also, 5,5'‐dithiobis(2‐nitrobenzoic acid; DTNB) was used as a substrate for the determination of both activities.…”

Section: Methodsmentioning

confidence: 99%

Synthesis and in silico studies of triazene‐substituted sulfamerazine derivatives as acetylcholinesterase and carbonic anhydrases inhibitors

Bilginer

Gül

Anil

et al. 2020

Archiv der Pharmazie

Self Cite

View full text Add to dashboard Cite

A novel series of sulfonamides, 4‐(3‐phenyltriaz‐1‐en‐1‐yl)‐N‐(4‐methyl‐2‐pyrimidinyl)benzenesulfonamides (1–9), was designed and synthesized by the diazo reaction between sulfamerazine and substituted aromatic amines for the first time. Their chemical structures were characterized by 1H nuclear magnetic resonance (NMR), 13C NMR, and high‐resolution mass spectra. The newly synthesized compounds were evaluated in terms of acetylcholineasterase (AChE) and human carbonic anhydrases (hCA) I and II isoenzymes inhibitory activities. According to the AChE inhibition results, the Ki values of the compounds 1–9 were in the range of 19.9 ± 1.5 to 96.5 ± 20.7 nM against AChE. Tacrine was used as the reference drug and its Ki value was 49.2 ± 2.7 nM against AChE. The Ki values of the compounds 1–9 were in the range of 10.2 ± 2.6 to 101.4 ± 27.8 nM against hCA I, whereas they were 18.3 ± 4.4 to 48.1 ± 4.5 nM against hCA II. Acetazolamide was used as a reference drug and its Ki values were 72.2 ± 5.4 and 52.2 ± 5.7 nM against hCA I and hCA II, respectively. The most active compounds, 1 (nonsubstituted) against AChE, 5 (4‐ethoxy‐substituted) against hCA I, and 8 (4‐bromo‐substituted) against hCA II, were chosen and docked at the binding sites of these enzymes to explain the inhibitory activities of the series. The newly synthesized compounds presented satisfactory pharmacokinetic properties via the estimation of ADME properties.

show abstract

Investigation of inhibitory properties of some hydrazone compounds on hCA I, hCA II and AChE enzymes

Cited by 130 publications

References 78 publications

The inhibition profile of sesamol against α-glycosidase and acetylcholinesterase enzymes

The inhibition profile of sesamol against α-glycosidase and acetylcholinesterase enzymes

Supramolecular complexes of Ni (II) and Co (II) 4‐aminobenzoate with 3‐cyanopyridine: Synthesis, spectroscopic characterization, crystal structure, and enzyme inhibitory properties

Synthesis and in silico studies of triazene‐substituted sulfamerazine derivatives as acetylcholinesterase and carbonic anhydrases inhibitors

Contact Info

Product

Resources

About