Synthesis and bioactivities of pyrazoline benzensulfonamides as carbonic anhydrase and acetylcholinesterase inhibitors with low cytotoxicity

Ozgun, Dilan Ozmen; Gül, Halise İnci; Yamalı, Cem; Sakagami, Hiroshi; Gülçın, İlhami; Şüküroğlu, Murat; Supuran, Claudiu T.

doi:10.1016/j.bioorg.2018.12.028

Cited by 116 publications

(43 citation statements)

References 42 publications

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“…[7,67] Preferred AChE inhibitors for treating AD are inhibitors that increase the activity of cholinergic neurotransmission by increasing the amount of ACh. [68,69] As the most potent inhibitor, the long-acting tacrine (IC 50 : 8.18 nM; K i : 8.59 ± 5.38 nM) compound has a hepatotoxic effect. In particular, it was found that the liver enzyme increases alanine transaminase level.…”

Section: Resultsmentioning

confidence: 99%

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

Topal

2019

International Journal of Food Properties

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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

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Section: Resultsmentioning

confidence: 99%

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

Topal

2019

International Journal of Food Properties

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“…As of now, there is no FDA-recognized adjuvant therapy for this outcome [6]. In this vein, several compounds, especially derivatives of β-amino carbonyl and pyrazoline benzensulfonamides, have been considered as in vitro cytotoxicity-enhancing drug candidates and also CA inhibitor candidates in OSCC cell lines (i.e., Ca9-22, HSC-2, HSC-3, and HSC-4) [43,44,45].…”

Section: Resultsmentioning

confidence: 99%

Dissecting the Proton Transport Pathway in Oral Squamous Cell Carcinoma: State of the Art and Theranostics Implications

Lorenzo-Pouso

Pérez‐Sayáns

Zorrilla

et al. 2019

IJMS

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Cancer cells overexpress proton exchangers at the plasma membrane in order acidify the extracellular matrix and maintain the optimal pH for sustaining cancer growth. Among the families of proton exchangers implicated in carcinogenesis, carbonic anhydrases (CAs), monocarboxylate transporters (MCTs), Na+/H+ exchangers (NHEs), sodium bicarbonate cotransporters (NBCs), and vacuolar ATPases (V-ATPases) are highlighted. Considerable research has been carried out into the utility of the understanding of these machineries in the diagnosis and prognosis of several solid tumors. In addition, as therapeutic targets, the interference of their functions has contributed to the discovery or optimization of cancer therapies. According to recent reports, the study of these mechanisms seems promising in the particular case of oral squamous cell carcinoma (OSCC). In the present review, the latest advances in these fields are summarized, in particular, the usefulness of proton exchangers as potential prognostic biomarkers and therapeutic targets in OSCC.

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“…This enzyme terminates nerve conduction by hydrolyzing acetylcholine (ACh) to acetic acid and choline (Ch) in the cholinergic synapses of the nervous system, somatic system, and central nervous system. The AChE inhibitors are clinically used for the treatment of AD, which increase cholinergic functions in cholinergic synapses …”

Section: Introductionmentioning

confidence: 99%

Investigation of the effects of some sulfonamides on acetylcholinesterase and carbonic anhydrase enzymes

Köksal

Alım

Bayrak

et al. 2019

J Biochem & Molecular Tox

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Human carbonic anhydrase I and II isoenzymes (hCA I and II) and acetylcholinesterase (AChE) are important metabolic enzymes that are closely associated with various physiological and pathological processes. In this study, we investigated the inhibition effects of some sulfonamides on hCA I, hCA II, and AChE enzymes. Both hCA isoenzymes were purified by Sepharose-4B-L-Tyrosine-5-amino-2-methylbenzenesulfonamide affinity column chromatography with 1393.44 and 1223.09folds, respectively. Also, some inhibition parameters including IC 50 and K i values were determined. Sulfonamide compounds showed IC 50 values of in the range of 55.14 to 562.62 nM against hCA I, 55.99 to 261.96 nM against hCA II, and 98.65 to 283.31 nM against AChE. K i values were in the range of 23.40 ± 9.10 to 365.35 ± 24.42 nM against hCA I, 45.87 ± 5.04 to 230.08 ± 92.23 nM against hCA II, and 16.00 ± 45.53 to 157.00 ± 4.02 nM against AChE. As a result, sulfonamides had potent inhibition effects on these enzymes. Therefore, we believe that these results may contribute to the development of new drugs particularly in the treatment of some disorders. K E Y W O R D Sacetylcholinesterase, carbonic anhydrase, enzyme inhibition, sulfonamides

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Synthesis and bioactivities of pyrazoline benzensulfonamides as carbonic anhydrase and acetylcholinesterase inhibitors with low cytotoxicity

Cited by 116 publications

References 42 publications

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

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

Dissecting the Proton Transport Pathway in Oral Squamous Cell Carcinoma: State of the Art and Theranostics Implications

Investigation of the effects of some sulfonamides on acetylcholinesterase and carbonic anhydrase enzymes

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