Discovery of Potent Carbonic Anhydrase and Acetylcholinesterase Inhibitors: 2-Aminoindan β-Lactam Derivatives

Genc, Hayriye; Kalın, Ramazan; Köksal, Zeynep; Sadeghian, Nastaran; Koçyiğit, Ümit M.; Zengin, Mustafa; Gülçın, İlhami; Özdemir, Haşan

doi:10.3390/ijms17101736

Cited by 69 publications

(20 citation statements)

References 75 publications

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“…In order to the check the purity of the enzyme and determine its molecular weight (MW), the pooled enzyme from gel filtration chromatography was applied to SDS-PAGE according to Laemmli's procedure [45] as described previously in detail. [46][47][48] Discontinuous electrophoresis was conducted by using 12.5% and 4% stacking gel. The gel was stained in Coomassie Blue and afterwards it was washed.…”

Section: Determination Of Pod Activitymentioning

confidence: 99%

Purification and selected biochemical properties of peroxidase from cress (Lepidium sativum sub sp. sativum)

Altay

Köktepe

Durmaz

et al. 2018

International Journal of Food Properties

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Cress (Lepidium sativum) is an annual herb from Brassicaceae family, and in some regions. It is known as peppergrass, garden cress, garden peppercress, pepperwort, or poor man's pepper. Cress is an important medicinal plant in some countries including Turkey. This plant has major scientific and therapeutic significance. Peroxidase (POD, E.C.1.11.1.7) is an oxidoreductase enzyme produced by a number of organisms. In this study, POD enzyme was purified from cress by ammonium sulphate precipitation, gel filtration, and CM-Sephadex ion-exchange chromatographies. K m and V max values were calculated from the Lineweaver-Burk graph for H 2 O 2 and guaiacol substrates and the substrate specificity of POD was investigated. The results showed that substrate specificity of H 2 O 2 is better than substrate specificity of guaiacol for this enzyme. The inhibition effects of three cations (Al 3+ , Cu 2+ , and Cr 3+) and one organic compound of cetyl trimethylammonium bromide were performed and their inhibition types were determined. Finally, optimum pH, optimum temperature, optimum ionic strength, and stable pH were determined.

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Section: Determination Of Pod Activitymentioning

confidence: 99%

Purification and selected biochemical properties of peroxidase from cress (Lepidium sativum sub sp. sativum)

Altay

Köktepe

Durmaz

et al. 2018

International Journal of Food Properties

Self Cite

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“…Additionally, CA enzymes take part in vital functions such as diversity and workability [7][8][9][10] (Table 1), remarkable activities against CA I, and CA II in the ranges of 1.27-3.30 nM and 1.1-2.68 nM, respectively, were obtained.…”

Section: Cholinergic Enzymes Assaymentioning

confidence: 99%

“…CA first purified from bovine erythrocytes [6,7], are found in tissues such as brain, lung, stomach, pancreas, liver, kidney, muscle tissue, and especially red blood cells [8,9]. It is one of the most important buffer systems in human body.…”

Section: Previous Studiesmentioning

confidence: 99%

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Inhibition Effects of Some Lignans on Carbonic Anhydrase, Acetylcholinesterase and Butyrylcholinesterase Enzymes Leyla Polat Köse and İlhami Gülçin

Köse¹,

Gülçın²

2017

Rec.Nat.Prod.

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Lignans are a large group of chemical compounds found in plants. They have effects on enzymes, protein synthesis, cell proliferation, angiogenesis, growth factor and cell differentiation. In this study, inhibition effects of α-(-)-conidendrin, enterodiole, enterolactone, nordihydroguaiaretic acid, secoisolariciresinol and secoisolariciresinol diglucoside against carbonic anhydrase I and II isoenzymes (CA I, and II) and acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes were investigated. The Ki values of the lignans were found to be in the ranges of 1.27-3.30 nM for CA I, 1.11-2.68 nM for CA II, 0.72-1.62 nM for AChE, and 0.08-0.20 nM for AChE.

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“…Alzheimer's disease (AD) plays a crucial rule in dementia, affecting millions of people around the world, according to the Alzheimer's World Report [1]. The treatment of Alzheimer's disease symptoms is based on inhibiting the cholinesterase enzymes (ChEs) which exist in the central nervous system [2,3]. To design a new, and safe pharmaceutical drug with long half-live time, high bioavailability, and high efficacy with less toxicity is a challenge in pharmaceutical research.…”

Section: Introductionmentioning

confidence: 99%

Synthesis, X-ray Single Crystal, Conformational Analysis and Cholinesterase Inhibitory Activity of a New Spiropyrrolidine Scaffold Tethered Benzo[b]Thiophene Analogue

et al. 2020

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Described herein is a one-pot protocol for the synthesis of a substituted spiropyrrolidine scaffold tethered benzo [b]thiophene analogue from (E)-3-(benzo[b]thiophen-2-yl)-1-(4-fluoro-phenyl)prop-2-en-1-one. The described protocol has the advantage of the high purity of the cyclized adduct and high chemical yield. To assign the chemical structure, different spectrophotometric tools have been applied, including 1 H-NMR, 13 C-NMR, FTIR, and the X-ray single crystal technique. The X-ray structure showed that the studied compound exist in two disordered parts with equal partial occupancies. The energies of the two conformers were found to be very similar and not exceed 1 kcal/mol, which justifies their coexistence in the crystal with equal percentage. The molecular packing in the crystal was analyzed using Hirshfeld topology analysis. The packing described as two dimensional hydrogen bond network extended along the ac-plane in both conformers but the intermolecular interactions included in each conformer are not similar. The synthesized spiropyrrolidine scaffold tethered benzo[b]thiophene analogue was examined against cholinesterase inhibitory activity and show moderate activity compared to standard drug galantamine. a wide range of pharmaceutical applications, including anti-cancer drugs, and also in the material chemistry applications [6]. Some examples of commercially available compounds that contains the benzo[b]thiophene core structure are: raloxifene [7] (trade name: Evista; as anti-cancer agent for breast cancer), sertaconazole [8], zileuton [9] and tamoxifen [10]. Additionally, several reports have disclosed the importance in medicinal chemistry of the benzo[b]thiophene scaffold which can act as an inhibitor for acetyl-CoA carboxylase [11], tubulin polymerisation [12,13], and also as a modulator for the estrogen receptor [14]. On the other hand, benzo[b]thiophenes have been used as anticonvulsant [15], antidepressant, antidiabetic [16], anti-tubercular [17], anti-fungal [18], enzyme inhibitor [19], and anti-malarial drugs [20], and are used in asthma treatment too [8].In this paper we combined different pharmacophores including spiroindoline, pyrrole, thiazole, and benzo[b]thiophene moieties into one molecule which has been assessed in vitro for its AChE enzyme inhibition for AD treatment. The structure of the newly synthesized compound was confirmed using the single crystal X-ray diffraction technique. Hirshfeld topology analysis of molecular packing was performed to determine the different intermolecular contacts in the crystal structure. DFT calculations were carried out to study the structural aspects of the studied compound.

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Discovery of Potent Carbonic Anhydrase and Acetylcholinesterase Inhibitors: 2-Aminoindan β-Lactam Derivatives

Cited by 69 publications

References 75 publications

Purification and selected biochemical properties of peroxidase from cress (Lepidium sativum sub sp. sativum)

Purification and selected biochemical properties of peroxidase from cress (Lepidium sativum sub sp. sativum)

Inhibition Effects of Some Lignans on Carbonic Anhydrase, Acetylcholinesterase and Butyrylcholinesterase Enzymes Leyla Polat Köse and İlhami Gülçin

Synthesis, X-ray Single Crystal, Conformational Analysis and Cholinesterase Inhibitory Activity of a New Spiropyrrolidine Scaffold Tethered Benzo[b]Thiophene Analogue

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