Kurumun Atıf Alan Makalesi
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Investigation of inhibitory properties of some hydrazone compounds on hCA I, hCA II and AChE enzymes
Scopus
Toplam 153 atıf DOI
Recently, inhibition of carbonic anhydrase (hCA) and acetylcholinesterase (AChE) have appeared as a promising approach for pharmacological intervention in a variety of disorders such as glaucoma, epilepsy, obesity, cancer, and Alzheimer's disease. Keeping this in mind, N,N′-bis[(1-aryl-3-heteroaryl)propylidene]hydrazine dihydrochlorides, N1-N11, P1, P4-P8, and R1-R6, were synthesized to investigate their inhibitory activity against hCA I, hCA II, and AChE enzymes. All compounds in N, P, and R-series inhibited hCAs (I and II) and AChE more efficiently than the reference compounds acetazolamide (AZA), and tacrine. According to the activity results, the most effective inhibitory compounds were in R-series with the K i values of 203 ± 55–473 ± 67 nM and 200 ± 34–419 ± 94 nM on hCA I, and hCA II, respectively. N,N′-Bis[1-(4-fluorophenyl)-3-(morpholine-4-yl)propylidene]hydrazine dihydrochlorides, N8, in N-series, N,N′-Bis[1-(4-hydroxyphenyl)-3-(piperidine-1-yl)propylidene]hydrazine dihydrochlorides, P4, in P-series, and N,N′-bis[1-(4-chlorophenyl)-3-(pyrrolidine-1-yl)propylidene]hydrazine dihydrochlorides, R5, in R-series were the most powerful compounds against hCA I with the K i values of 438 ± 65 nM, 344 ± 64 nM, and 203 ± 55 nM, respectively. Similarly, N8, P4, and R5 efficiently inhibited hCA II isoenzyme with the K i values of 405 ± 60 nM, 327 ± 80 nM, and 200 ± 34 nM, respectively. On the other hand, P-series compounds had notable inhibitory effect against AChE than the reference compound tacrine and the K i values were between 66 ± 20 nM and 128 ± 36 nM. N,N′-Bis[1-(4-fluorophenyl)-3-(piperidine-1-yl)propylidene]hydrazine dihydrochlorides, P7, was the most potent compound on AChE with the K i value of 66 ± 20 nM. The other most promising compounds, N,N′-bis[1-(4-hydroxyphenyl)-3-(morpholine-4-yl)propylidene]hydrazine dihydrochlorides, N4 in N-series and N,N′-bis[1-(4-hydroxyphenyl)-3-(pyrrolidine-1-yl)propylidene]hydrazine dihydrochlorides, R4 in R-series were againts AChE with the K i values of 119 ± 20 nM, 88 ± 14 nM, respectively.
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Atıf Yapan Yayın
Integrated chemical and biological analysis of Astragalus aintabicus Boiss extracts using chromatographic profiling, in vitro assays, and in Silico modeling
Scopus
Havuzumuzda 2 atıf almış
Astragalus aintabicus Boiss, an endemic and little-studied species native to Turkey, has been extensively studied for its phytochemical composition and biological activities. Various plant parts (flowers, roots and aerial parts) were subjected to sequential extraction with solvents of increasing polarity (ethyl acetate, ethanol, ethanol/water and water). Phytochemical profiling by high-performance liquid chromatography coupled with electrospray ionisation quadrupole time-of-flight mass spectrometry (HPLC-ESI-Q-TOF-MS) revealed that the aerial parts, especially those extracted with ethanol and ethanol/water, were rich in phenolic compounds and flavonoids, with vanillic acid and hyperoside identified as predominant constituents. In contrast, the flower and root extracts had a lower content of phytochemicals, with 4-hydroxybenzoic acid being the most important compound. The antioxidant potential of the extracts was evaluated using various free radical scavenging and reduction assays, with the aerial leaf extracts showing the strongest activity. Enzyme inhibition assays showed that the extracts from the aerial leaves had the strongest inhibitory effects against acetylcholinesterase (AChE), butyrylcholinesterase (BChE) and α-amylase, while the flower extracts were more effective inhibitors of tyrosinase and α-glucosidase. Cytotoxicity tests showed a moderate anticancer potential of the extracts with IC₅₀ value between 13.01 and 141.20 µg/ml, but with limited selectivity against cancer cells (HEK-293, A549, DU-145, HELA). In silico molecular docking studies, supported by molecular dynamics (MD) simulations and MM/PBSA (molecular mechanics-Poisson–Boltzmann surface area) free energy calculations, revealed a strong binding affinity of key phytoconstituents, rutin, isoquercitrin, hyperoside and kaempferol to important therapeutic protein targets. Overall, the results suggest that A. aintabicus, especially its aerial parts, is a promising source of bioactive compounds with antioxidant, enzyme inhibitory and moderate cytotoxic properties, warranting further investigation for its potential applications in the pharmaceutical and nutraceutical sectors.
Atıf Yapan Makale Bilgileri
Kurumlar (8)
Bingöl Üniversitesi
Bingol, Turkey
Consiglio Nazionale delle Ricerche
Rome, Italy
Harran Üniversitesi
Sanliurfa, Turkey
İstanbul Arel Üniversitesi
Istanbul, Turkey
Şanlıurfa Provincial Directorate of National Education
Sanliurfa, Turkey
Selçuk Üniversitesi
Selçuklu, Turkey
Università degli Studi di Camerino
Camerino, Italy
University of Novi Sad
Novi Sad, Serbia