The first synthesis, carbonic anhydrase inhibition and anticholinergic activities of some bromophenol derivatives with S including natural products

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Atıf İçin Kopyala

BAYRAK C., TASLIMI P., KARAMAN H. S., GÜLÇİN İ., MENZEK A.

BIOORGANIC CHEMISTRY, cilt.85, ss.128-139, 2019 (SCI-Expanded)

• Yayın Türü: Makale / Tam Makale
• Cilt numarası: 85
• Basım Tarihi: 2019
• Doi Numarası: 10.1016/j.bioorg.2018.12.012
• Dergi Adı: BIOORGANIC CHEMISTRY
• Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
• Sayfa Sayıları: ss.128-139
• Anahtar Kelimeler: Bromination, Bromophenol, Carbonic anhydrase, Acetylcholinesterase, Enzyme inhibition, Molecular docking, ERYTHROCYTE ISOZYMES I, ISOENZYMES I, ACETYLCHOLINE ESTERASE, ANTIOXIDANT PROPERTIES, BIOLOGICAL EVALUATION, METHYL ETHERS, MANNICH-BASES, BUTYRYLCHOLINESTERASE, PROFILES, ALGA
• Atatürk Üniversitesi Adresli: Evet

Özet

Starting from vanillin, known four benzyl bromides with Br were synthesized. The first synthesis of natural product 3,4-dibromo-5-((methylsulfonyl)methyl)benzene-1,2-diol (2) and 3,4,6-tribromo-5-((methylsulfonyl) methyl)benzene-1,2-diol (3) and derivatives were carried out by demethylation, acetylatilation, oxidation and hydrolysis reactions of the benzyl bromides. Also, these compounds were tested against some important enzymes like acetylcholinesterase and butyrylcholinesterase enzymes, carbonic anhydrase I, and II isoenzymes. The novel bromophenols showed Ki values of in range of 53.75 +/- 12.54-234.68 +/- 46.76 nM against hCA I, 42.84 +/- 9.36 and 200.54 +/- 57.25 nM against hCA II, 0.84 +/- 0.12-14.63 +/- 3.06 nM against AChE and 0.93 +/- 0.20-18.53 +/- 5.06 nM against BChE. Induced fit docking process performed on the compounds inhibiting hCA I, hCA II, AChE, and BChE receptors. Hydroxyl group should exist at the aromatic ring of the compounds for inhibition of the enzymes. The moieties reported in this study will be useful for design of more potent and selective inhibitors against the enzymes.