The investigation of the interaction between orientin and bovine serum albumin by spectroscopic analysis

Toprak M., ARIK M.

LUMINESCENCE, cilt.29, sa.7, ss.805-809, 2014 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 29 Sayı: 7
  • Basım Tarihi: 2014
  • Doi Numarası: 10.1002/bio.2624
  • Dergi Adı: LUMINESCENCE
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.805-809
  • Anahtar Kelimeler: fluorescence quenching, orientin, bovine serum albumin, FLUORESCENCE SPECTROSCOPY, HYDROCHLORIDE, FLAVONOIDS, LIPOSOMES, BINDING
  • Atatürk Üniversitesi Adresli: Evet

Özet

In this paper, the interaction between orientin and bovine serum albumin (BSA) was examined using fluorescence and absorbance spectroscopy. The analysis of the quenching mechanism was done using Stern-Volmer plots which exhibit upward (positive) deviation. A linear response to orientin was shown in the concentration range between 3 and 50 mu M. The experimental results showed the presence of a static quenching process between orientin and BSA. The thermodynamic parameters Delta H, Delta S and Delta G were also calculated and suggested that the hydrophobic and electrostatic interactions played an important role in the interaction between orientin and BSA. Furthermore, the distances between BSA and orientin were determined according to Forster non-radiation energy transfer theory. In addition, the results of the synchronous fluorescence obtained indicated that the binding of orientin with BSA could affect conformation in BSA. Copyright (C) 2013 John Wiley & Sons, Ltd.