Synthesis of oxazolidinone from enantiomerically enriched allylic alcohols and determination of their molecular docking and biologic activities

Atmaca, Ufuk; Kaya, Rüya; Karaman, Halide Sedef; Çelik, M.

doi:10.1016/j.bioorg.2019.102980

Cited by 56 publications

(19 citation statements)

References 81 publications

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“…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: 81%

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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: Resultssupporting

confidence: 81%

“…It prevents the breakdown of complex carbohydrates. [48][49][50] Sesame (Sesamum indicum L.) is one of the most important seeds used in oil. Protein and fat contents are very high.…”

Section: Introductionmentioning

confidence: 99%

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

Topal

2019

International Journal of Food Properties

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“…Also, it was reported that sulfonylated amino acid hydroxamates act as efficient CAIs The rapid, physiologically most relevant cytosolic isozyme CA II is highly active cytosolic isoform and is abundant in most cells . As shown in Table , the inhibition effects of novel bis‐sulfone derivatives ( 2a‐2j ) against a dominant cytosolic isoform of hCA II were revealed to be quite similar to that shown toward physiologically relevant CA I.…”

Section: Resultsmentioning

confidence: 99%

Synthesis of novel bis‐sulfone derivatives and their inhibition properties on some metabolic enzymes including carbonic anhydrase, acetylcholinesterase, and butyrylcholinesterase

Biçer

Kaya

Anil

et al. 2019

J Biochem & Molecular Tox

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In this study, a series of novel bis-sulfone compounds (2a-2j) were synthesized by oxidation of the bis-sulfides under mild reaction conditions. The bis-sulfone derivatives were characterized by 1 H-NMR, 13 C-NMR, Fourier-transform infrared spectroscopy, and elemental analysis techniques. Nuclear Overhauser effect experiments were performed to determine the orientation of the sulfonyl groups in bis-sulfone derivatives. Here, we report the synthesis and testing of novel bis-sulfone compound-based hybrid scaffold of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibitors for the development of novel molecules toward the therapy of Alzheimer's disease. The novel synthesized bis-sulfone compounds demonstrated K i values between 11.4 ± 3.4 and 70.7 ± 23.2 nM on human carbonic anhydrase I isozyme (hCA I), 28.7 ± 6.6 to 77.6 ± 5.6 nM on human carbonic anhydrase II isozyme (hCA II), 18.7 ± 2.61 to 95.4 ± 25.52 nM on AChE, and 9.5 ± 2.1 to 95.5 ± 1.2 nM on BChE enzymes. The results showed that novel bissulfone derivatives can have promising drug potential for glaucoma, leukemia, epilepsy, and Alzheimer's disease, which are associated with the high enzymatic activity of hCA I, hCA II, AChE, and BChE enzymes. K E Y W O R D S acetylcholinesterase, bis-sulfide, butyrylcholinesterase, bis-sulfone, carbonic anhydrase

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“…Hence, the crystal structure has been repaired and prepared with protein preparation wizard module of Schrodinger Maestro 12.0 before using in binding site prediction and induced-fit docking studies. The workflow that includes a detailed description of previous studies [48,49] was described in the overview. Bond order and charges were assigned and then missing hydrogen atoms were added to crystal structure.…”

Section: Ligand Preparation and Pharmacokinetic Properties Predictionmentioning

confidence: 99%

N‐Substituted pyrimidinethione and acetophenone derivatives as a new therapeutic approach in diabetes

Taslimi

Sujayev

Karaman

et al. 2020

Archiv der Pharmazie

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In this study, compounds with 4‐hydroxybutyl, 4‐phenyl, 5‐carboxylate, and pyrimidine moieties were determined as α‐glycosidase inhibitors. N‐Substituted pyrimidinethione and acetophenone derivatives (A1–A5, B1–B11, and C1–C11) were good inhibitors of the α‐glycosidase enzyme, with Ki values in the range of 104.27 ± 15.75 to 1,004.25 ± 100.43 nM. Among them, compound B7 was recorded as the best inhibitor, with a Ki of 104.27 ± 15.75 nM against α‐glycosidase. In silico studies were carried out to clarify the binding affinity and interaction mode of the compounds with the best inhibition score against α‐glycosidase from Saccharomyces cerevisiae. Compounds B7 (S) and B11 (R) exhibited a good binding affinity with docking scores of −8.608 and 8.582 kcal/mol, respectively. The docking results also showed that the 4‐hydroxybutyl and pyrimidinethione moieties play a key role in S. cerevisiae and human α‐glycosidase inhibition.

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Synthesis of oxazolidinone from enantiomerically enriched allylic alcohols and determination of their molecular docking and biologic activities

Cited by 56 publications

References 81 publications

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

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

Synthesis of novel bis‐sulfone derivatives and their inhibition properties on some metabolic enzymes including carbonic anhydrase, acetylcholinesterase, and butyrylcholinesterase

N‐Substituted pyrimidinethione and acetophenone derivatives as a new therapeutic approach in diabetes

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