Voltammetric and Spectroscopic Evaluation of the Interactions of (E)-1-((4-phenoxyphenylimino)methyl)naphthalen-2-ol with Bovine and Human Serum Albumins at Physiological pH

Biçer E., TANJU N. Ö., Macit M.

RUSSIAN JOURNAL OF ELECTROCHEMISTRY, vol.58, no.9, pp.835-843, 2022 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 58 Issue: 9
  • Publication Date: 2022
  • Doi Number: 10.1134/s1023193522090038
  • Journal Name: RUSSIAN JOURNAL OF ELECTROCHEMISTRY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Aqualine, Chemical Abstracts Core, Chimica, Compendex, Environment Index, INSPEC
  • Page Numbers: pp.835-843
  • Keywords: Schiff base, serum albumins, interaction, voltammetry, spectroscopy, GLASSY-CARBON ELECTRODE, MOLECULAR DOCKING, VISUAL PIGMENTS, SCHIFF-BASES, DRUG, BINDING, FLUORESCENCE, PROTEINS, AFFINITY, BEHAVIOR
  • Ondokuz Mayıs University Affiliated: Yes

Abstract

The bindings of (E)-1-((4-phenoxyphenylimino)methyl)naphthalen-2-ol (PMNO) to bovine and human serum albumins (abbreviated as BSA and HSA, respectively) in 0.05 M phosphate buffer (abbreviated as PB) solution of pH 7.40 were analysed via square-wave voltammetry (SWV) and UV-Vis absorption spectroscopy. By using decreases in the reduction current of PMNO with addition of the serum albumins, the binding constants of the interactions between PMNO and BSA and HSA for a binding ratio of 1 : 1 were found to be 1.97 x 10(8) and 1.78 x 10(6) M-1, respectively. From the UV-Vis absorption spectroscopy data at 443 nm, the binding constant values for PMNO-BSA and PMNO-HSA systems were obtained to be 1.37 x 10(7) and 1.39 x 10(6) M-1, respectively.