Inhibitory Effects and Kinetic-Docking Studies of Xanthohumol From Humulus lupulus Cones Against Carbonic Anhydrase, Acetylcholinesterase, and Butyrylcholinesterase


AYDIN T., ŞENTÜRK M., KAZAZ C., ÇAKIR A.

NATURAL PRODUCT COMMUNICATIONS, cilt.14, sa.10, 2019 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 14 Sayı: 10
  • Basım Tarihi: 2019
  • Doi Numarası: 10.1177/1934578x19881503
  • Dergi Adı: NATURAL PRODUCT COMMUNICATIONS
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Anahtar Kelimeler: Humulus lupulus L., xanthohumol, molecular docking, carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase, enzyme inhibition, IN-VITRO INHIBITION, FLAVONOIDS, BINDING, SITE
  • Atatürk Üniversitesi Adresli: Evet

Özet

Xanthohumol is an essential prenyl flavonoid of Humulus lupulus L. cones, and the taste of beer is due to this compound. Lately, xanthohumol has earned significant interest due to its potential anticancer, antigenotoxic, and adipogenesis effects. In this paper, the inhibitory effects of xanthohumol on human carbonic anhydrase isozymes (hCAI and hCAII), acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) were studied. Also, molecular docking studies were used to investigate ligand interaction diagrams of xanthohumol at the binding cavities of hCAI and II. Xanthohumol was isolated from hop cones by silica gel column chromatography. Carbonic anhydrase enzyme activities were determined spectrophotometrically. In addition, molecular modeling approaches were used for the hCAI and hCAII isoenzymes. Ellman's method was used for the inhibitor activities of AChE and BChE. The K-I values of xanthohumol were detected as 0.085 mu M for hCAI, 0.049 mu M for hCAII, 95.5 nM for AChE, and 124.9 nM for BChE. In conclusion, xanthohumol can pleiotropically exert health promoting effects. It has antiglaucoma, anticonvulsant, antiepileptic, and anticancer activities due to its potent inhibitory effects on hCAI and hCAII. These findings may open new avenues for the design and development of novel hCAI, hCAII, AChE, and BChE inhibitors compared with sulfonamide/sulfamate.