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akaturk Akademik ölçüm

Makale detayı · 2024

Structure-based inhibition of acetylcholinesterase and butyrylcholinesterase with 2-Aryl-6-carboxamide benzoxazole derivatives: synthesis, enzymatic assay, and in silico studies

Dergi

Molecular Diversity

ISSN 1381-1991

YÖKSİS OpenAlex Açık erişim · gold SJR Q2 JCR Q2 Atıf 20 Üst %10 Yüzdelik 97.2% FWCI 6.28
Yıl
2024
Tür
article

Veri kaynağı ayrımı

  • YÖKSİS YÖKSİS makale kaydı
  • YÖKSİS dergi adı Molecular Diversity
  • Katalog eşleşmesi (ISSN) Molecular Diversity
  • OpenAlex OpenAlex zenginleştirmesi (özet, atıf, konular)

Özet

OpenAlex · İngilizce

Hamamelitannin (2′,5-di-O-galloyl-hamamelose) bears two-gallate moieties in its structure, and is a natural phenolic product in the leaves and the bark of Hamamelis virginiana. The antioxidant capacity of hamamelitannin was evaluated by a range of methods, with the following findings: the ability to reduce potassium ferric cyanide; the scavenging of N,N-dimethyl-p-phenylenediamine dihydrochloride radical (DMPD•+); the scavenging of 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulphonate) radical (ABTS•+); the scavenging of 1,1-diphenyl-2-picrylhydrazyl radical (DPPH•); and the ability to reduce cupric ions (Cu2+). Additionally, reference antioxidants of α-Tocopherol, butylated hydroxyanisole (BHA), Trolox, and butylated hydroxytoluene (BHT) were used for comparison. For DPPH radical scavenging, hamamelitannin had an IC50 value of 19.31 μg/mL, while the IC50 values for BHA, BHT, Trolox, and α-Tocopherol were 10.10, 25.95, 7.05, and 11.31 μg/mL, respectively. The study found that hamamelitannin functioned similarly to BHA, α-tocopherol, and Trolox in terms of DPPH• scavenging, but better than BHT. Additionally, as a polyphenolic secondary metabolite, the hamamelitannin inhibition capability of several metabolic enzymes was demonstrated, including acetylcholinesterase (AChE), butyrylcholinesterase (BChE), carbonic anhydrase I (CA I), carbonic anhydrase II (CA II) and α-glycosidase. The Ki values of hamamelitannin exhibited 7.40, 1.99, 10.18, 18.26, and 25.79 nM toward AChE, BChE, hCA I, hCA II, and α-glycosidase, respectively.

Konular

Atıflar

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20 atıf

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Yazarlar

  1. BURAK KUZU
  2. MEHMET ABDULLAH ALAGÖZ
  3. YELİZ DEMİR
  4. İLHAMİ GÜLÇİN ATATÜRK ÜNİVERSİTESİ
  5. SERDAR BURMAOĞLU
  6. ÖZTEKİN ALGÜL
  7. LOKMAN DURMAZ ERZİNCAN BİNALİ YILDIRIM ÜNİVERSİTESİ
  8. PARHAM TASLIMI BARTIN ÜNİVERSİTESİ