Enzalutamide-human serum albumin interaction: Electrochemical exploration of complex formation and binding parameters


Chenguiti F., Bakirhan N. K., GÖZELLE M., Doulache M., Saidat B., Atici E. B., ...Daha Fazla

Microchemical Journal, cilt.201, 2024 (SCI-Expanded) identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 201
  • Basım Tarihi: 2024
  • Doi Numarası: 10.1016/j.microc.2024.110760
  • Dergi Adı: Microchemical Journal
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, BIOSIS, CAB Abstracts, Chemical Abstracts Core, Chimica, Food Science & Technology Abstracts, Index Islamicus, Veterinary Science Database
  • Anahtar Kelimeler: Binding study, Electrochemical methods, Enzalutamide, Human serum albumin, Interaction
  • Gazi Üniversitesi Adresli: Evet

Özet

This research investigation employed electrochemical methods to explore the interaction between the anti-cancer drug Enzalutamide (ENZ) and Human Serum Albumin (HSA). Cyclic Voltammetry (CV), Differential Pulse Voltammetry (DPV), and Electrochemical Impedance Spectroscopy (EIS) techniques were used via a glassy carbon electrode (GCE) substrate. The interaction between ENZ and HSA was examined based on the changes in the electrochemical behavior of [Fe(CN)6]3−/4− redox species under physiological pH conditions. Electrochemical and kinetic parameters of the redox probe in the presence of HSA, ENZ, and the ENZ-HSA complex were calculated. The results showed significant differences in these parameters due to the formation of an electro-inactive complex between the protein and the drug. Binding parameters of ENZ-HSA, such as the binding constant and complex stoichiometry, were found, revealing the formation of a robust drug-albumin complex with a binding constant value of 2.7 × 108 M−1. A molecular docking study was conducted to examine the possible binding mode of ENZ and its interactions with HSA. This research provides valuable insights and can serve as a reference for future studies to enhance drug delivery systems.