Deciphering binding mechanism between bovine serum albumin and new pyrazoline compound K4.

Bozkurt E., Gül H. İ.

Luminescence : the journal of biological and chemical luminescence, cilt.35, ss.534-541, 2020 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 35
  • Basım Tarihi: 2020
  • Doi Numarası: 10.1002/bio.3762
  • Dergi Adı: Luminescence : the journal of biological and chemical luminescence
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Aerospace Database, Agricultural & Environmental Science Database, Analytical Abstracts, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Communication Abstracts, EMBASE, INSPEC, MEDLINE, Metadex, Veterinary Science Database, Civil Engineering Abstracts
  • Sayfa Sayıları: ss.534-541
  • Anahtar Kelimeler: bovine serum albumin, fluorescence quenching, FRET, pyrazoline, RESONANCE ENERGY-TRANSFER, FLUORESCENCE, DERIVATIVES, DOCKING, ANTICANCER
  • Atatürk Üniversitesi Adresli: Evet

Özet

The binding mechanism of a new and possible drug candidate pyrazoline derivative compound K4 and bovine serum albumin (BSA) was investigated in buffer solution (pH 7.4) using ultraviolet-visible light absorption and steady-state and synchronous fluorescence techniques. The fluorescence intensity of BSA was quenched in the presence of K4. The quenching process between BSA and K4 was examined at four different temperatures. Decrease of the quenching constants calculated using the Stern-Volmer equation and at increasing temperature suggested that the interaction BSA-K4 was realized through a static quenching mechanism. Synchronous fluorescence measurements suggested that K4 bounded to BSA at the tryptophan region. Fourier transform infrared spectroscopy results showed that there was no significant change in polarity around the tryptophan residue The forces responsible for the BSA-K4 interaction were examined using thermodynamic parameters. In this study, the calculated negative value of Delta G, the negative value of Delta H and the positive value of Delta S pointed to the interaction being through spontaneous and electrostatic interactions that were dominant for our cases. This study provides a very useful in vitro model to researchers by mimicking in vivo conditions to estimate interactions between a possible drug candidate or a drug and body proteins.