Synthesis, characterization, anticancer, antimicrobial and carbonic anhydrase inhibition profiles of novel (3a R ,4 S ,7 R ,7a S )-2-(4-(( E )-3-(3-aryl)acryloyl) phenyl)-3a,4,7,7a-tetrahydro-1H-4,7-methanoisoindole-1,3(2H)-dione derivatives

Koçyiğit, Ümit M.; Budak, Yakup; Gürdere, Meliha Burcu; Teki̇n, Şaban; Köprülü, Tuğba Kul; Ertürk, Fatih; Özcan, Kezban; Gülçın, İlhami; Ceylan, Mustafa

doi:10.1016/j.bioorg.2016.12.001

Cited by 95 publications

(49 citation statements)

References 70 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Additionally, for this enzyme, natural phenolic compounds had K i values in the range of 2.98 ± 0.33–84.88 ± 40.32 nM. (iii)AChEIs are the most efficient approach to therapy the cognitive signs of AD and other important therapeutic applications in the treatment of ataxia, Parkinsonís disease, and senile dementia . In this paper, we investigated the AChE inhibitory potential of the natural phenolic compounds.…”

Section: Resultsmentioning

confidence: 99%

The impact of some natural phenolic compounds on carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase, and α‐glycosidase enzymes: An antidiabetic, anticholinergic, and antiepileptic study

Taslimi

Çağlayan

Gülçın

2017

J Biochem & Molecular Tox

144

View full text Add to dashboard Cite

Natural products from food and plant sources have been used for medicinal usage for ages. Also, natural products with therapeutic significance are compounds derived from animals, plants, or any microorganism. In this study, chrysin, carvacrol, hesperidin, zingerone, and naringin as natural phenols showed excellent inhibitory effects against human (h) carbonic anhydrase (CA) isoforms I and II (hCA I and II), α-glucosidase (α-Gly), acetylcholinesterase (AChE), and butyrylcholinesterase (BChE). These phenolic compounds were tested for the inhibition of α-glycosidase, hCA I, hCA II, AChE, and BChE enzymes and demonstrated efficient inhibition profiles with K values in the range of 3.70 ± 0.92-79.66 ± 20.81 nM against hCA I, 2.98 ± 0.33-84.88 ± 40.32 nM against hCA II, 4.93 ± 2.01-593.60 ± 134.74 nM against α-Gly, 0.52 ± 0.18-46.80 ± 17.15 nM against AChE, and 1.25 ± 0.22-32.08 ± 2.68 against BChE.

show abstract

Section: Resultsmentioning

confidence: 99%

The impact of some natural phenolic compounds on carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase, and α‐glycosidase enzymes: An antidiabetic, anticholinergic, and antiepileptic study

Taslimi

Çağlayan

Gülçın

2017

J Biochem & Molecular Tox

144

View full text Add to dashboard Cite

show abstract

“…Recently, the interactions of AChE and BChE with cyclic thioureas, hetaryl sulfonamides, Mannich bases, ureas derived from phenethylamines, tetrahydropyrimidines, diaryl ethers, β‐lactams, benzenesulfonamides, and tetrahydropyrimidine‐5‐carboxylates as well as the interactions for both CA isoenzymes with caffeic acid phenethyl ester, polyphenols and phenolic acids, benzotropones, bromophenols, dopaminergic compounds, sulfamides, sulfonamides, acylsulfonamides, benzenesulfonamides, 1,3,5‐trisubstituted‐pyrazolines,, tetralone‐based 1,4‐benzothiazepine derivatives, novel eugenol derivatives, some natural sulfonamide derivatives, and novel (3aR,4S,7R,7aS)‐2‐(4‐((E)‐3‐(3‐aryl)acryloyl) phenyl)‐3a,4,7,7a‐tetrahydro‐1H‐4,7‐methanoisoindole‐1,3(2H)‐dione derivatives benzylsulfamides have been studied.…”

Section: Discussionmentioning

confidence: 96%

Discovery of potent carbonic anhydrase, acetylcholinesterase, and butyrylcholinesterase enzymes inhibitors: The new amides and thiazolidine-4-ones synthesized on an acetophenone base

Taslimi

Osmanova

Gülçın

et al. 2017

J Biochem Mol Toxicol

View full text Add to dashboard Cite

Compounds containing nitrogen and sulfur atoms can be widely used in various fields, including industry, medicine, biotechnology, and chemical technology. Among them, amides of acids and heterocyclic compounds have an important place. These amides and thiazolidine-4-ones showed good inhibitory action against butyrylcholinesterase (BChE), acetylcholinesterase (AChE), and human carbonic anhydrase isoforms. AChE exists at high concentrations in the brain and red blood cells. BChE is an important enzyme that is plentiful in the liver, and it is released into the blood in a soluble form. They were demonstrated to have effective inhibition profiles with K values of 23.76-102.75 nM against hCA I, 58.92-136.64 nM against hCA II, 1.40-12.86 nM against AChE, and 9.82-52.77 nM against BChE. On the other hand, acetazolamide showed K value of 482.63 ± 56.20 nM against hCA I, and 1019.60 ± 163.70 nM against hCA II. Additionally, Tacrine inhibited AChE and BChE, showing K values of 397.03 ± 31.66 and 210.21 ± 15.98 nM, respectively.

show abstract

“…The Minimal Inhibitory Concentration (MIC) was performed by the diffusion disk test (Bauer, Kurby, Sherris, & Turck, ; Gülçİn, Kİreçcİ, Akkemİk, Topal, & Hİsar, ; Kocyigit et al, ; Tohma, Köksal, Kılıç, Alan, & Yılmaz, ). The standard strains used for analysis were Bacillus cereus (ATCC 11778), Escherichia coli (ATCC 25922), Listeria monocytogenes (ATCC 7644), Salmonella sp .…”

Section: Methodsmentioning

confidence: 99%

Characterization of lactobionic acid evidencing its potential for food industry application

Cardoso

Marques

Sotiles

et al. 2019

J Food Process Engineering

View full text Add to dashboard Cite

The chemical configuration of the lactobionic acid (LBA) evidences its potential properties, among which the antioxidant, antimicrobial, and chelating activities stand out in the literature. However, few studies aim at testing and confirming them. The purpose of this study was to determine some selected LBA properties, whose characteristics are of interest for its use as an ingredient in foodstuffs. The discussion followed the results of Fourier‐Transform Infrared Spectroscopy (FTIR), X‐ray diffractometry (XRD), 2,2‐diphenyl‐1‐picrylhydrazyl (DPPH) radical, 2,2′‐azino‐bis(3‐ethylbenzothiazoline‐6‐sulphonic acid) (ABTS) radical, thermogravimetric/derivative thermogravimetry (TGA/DTG), minimal inhibitory concentration (MIC) by the diffusion disk test, scanning electron microscopy (SEM), and iron/calcium chelating methodologies. The XRD analysis revealed the presence of an amorphous halo and the absence of defined peaks, a fact possibly related to its high hygroscopicity. The FTIR showed characteristic bands of the LBA structure. Results from TGA/DG verified the LBA thermal degradation, which evidenced that LBA could participate in most food industry unit processes within the first mass loss event. Antioxidant capacity reached a maximum inhibition of 56% for LBA and the chelating capacity of the iron ion achieved 54% of chelated ions, while the calcium ions reached 15%. The results revealed high potential of LBA application for microbial inhibition, moisture retention, and texture maintenance throughout storage of food products. Practical Applications Despite the potential of application of the LBA, few quantitative results demonstrate its ability of action in food. Even without permission in most countries around the world, more research with LBA will encourage the investigation of its toxicology, expanding the areas of application. Its thermal degradation profile and elevated solubility demonstrated the potential of LBA as food ingredient, performing moreover as antioxidant, chelating agent, antimicrobial, and texturizer. The results open the possibilities for many applications in the field of food chemistry and food industry.

show abstract

Synthesis, characterization, anticancer, antimicrobial and carbonic anhydrase inhibition profiles of novel (3a R ,4 S ,7 R ,7a S )-2-(4-(( E )-3-(3-aryl)acryloyl) phenyl)-3a,4,7,7a-tetrahydro-1H-4,7-methanoisoindole-1,3(2H)-dione derivatives

Cited by 95 publications

References 70 publications

The impact of some natural phenolic compounds on carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase, and α‐glycosidase enzymes: An antidiabetic, anticholinergic, and antiepileptic study

The impact of some natural phenolic compounds on carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase, and α‐glycosidase enzymes: An antidiabetic, anticholinergic, and antiepileptic study

Discovery of potent carbonic anhydrase, acetylcholinesterase, and butyrylcholinesterase enzymes inhibitors: The new amides and thiazolidine-4-ones synthesized on an acetophenone base

Characterization of lactobionic acid evidencing its potential for food industry application

Contact Info

Product

Resources

About