Bee venom and melittin: Potent key enzyme inhibitors with promising therapeutic potential

Alparslan B., Şentürk M., Erkan C.

Toxicon, cilt.252, 2024 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 252
  • Basım Tarihi: 2024
  • Doi Numarası: 10.1016/j.toxicon.2024.108164
  • Dergi Adı: Toxicon
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Aerospace Database, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, CAB Abstracts, Chemical Abstracts Core, Communication Abstracts, Environment Index, Metadex, Pollution Abstracts, Veterinary Science Database, Civil Engineering Abstracts
  • Anahtar Kelimeler: Bee venom, Carbonic anhydrase, Cholinesterases, Enzyme inhibition, Melittin, Neuraminidase
  • Van Yüzüncü Yıl Üniversitesi Adresli: Evet

Özet

Bee venom (BV) is a versatile product with extensive applications, boasting antibacterial and anticancer properties. Within this study, we focused on isolating melittin (Mel) from Apis mellifera L. venom and exploring the influence of both BV and Mel on specific enzymes, namely carbonic anhydrase (CA) I, CA II, CA IX, glutathione reductase (GR), acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and neuraminidase (NA). The rationale for selecting these enzymes is that their inhibitors have a particular interest in medicinal chemistry in the treatment of several diseases. BV was obtained using a poison collection apparatus, and Mel was isolated by means of High-Performance Liquid Chromatography (HPLC). All enzymes, except for CA I and CA II, were commercially sourced and of high purity, and the enzyme assays were carried out spectrophotometrically. Our findings showed that BV inhibited the enzymes with IC50 values of 0.583–3.32 ng/mL, and Mel showed an inhibition range of 0.528–3.2 ng/mL. These results underscore the potential therapeutic promise of BV and Mel as robust enzyme inhibitors, offering prospects for addressing diverse health conditions.