Investigation of neohesperidin dihydrochalcone binding to human serum albumin by spectroscopic methods


Bozoglan B. K., TUNÇ S., DUMAN O.

JOURNAL OF LUMINESCENCE, vol.155, pp.198-204, 2014 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 155
  • Publication Date: 2014
  • Doi Number: 10.1016/j.jlumin.2014.06.032
  • Journal Name: JOURNAL OF LUMINESCENCE
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.198-204
  • Keywords: Human serum albumin, Neohesperidin dihydrochalcone, Binding, Fluorescence spectroscopy, Synchronous fluorescence, Circular dichroism, HUMAN HEMOGLOBIN PROTEINS, FLUORESCENCE SPECTROSCOPY, CIRCULAR-DICHROISM, DRUGS, ACID, HYDROCHLORIDE, FLAVONOIDS, DEGRADATION, BERBERINE, WARFARIN
  • Akdeniz University Affiliated: Yes

Abstract

In this study, the interaction of human serum albumin (HSA) with neohesperidin dihydrochalcone (NHD) was investigated by UV, fluorescence, synchronous fluorescence and circular dichroism spectroscopic methods. Experimental results confirmed the complex formation between HSA and NHD molecules under physiological conditions. NHD quenched the intrinsic fluorescence spectrum of HSA by static quenching mechanism. The binding constant of this system was calculated as 2.79 x 10(4) M-1 at 298.15 K. The stability of HSA-NHD complex illustrated a decrease with increasing temperature. The number of binding sites was found to be 1. Thermodynamic parameter values were calculated by using van't Hoff equation. According to sign and magnitude of thermodynamic parameters (Delta H= -29.22 kJ mol(-1) and Delta S= -12.91 J mol(-1) K-1), hydrogen bonding and van der Waals forces were found as the effective interaction forces between HSA and NHD molecules. Synchronous fluorescence and circular dichroism spectroscopic methods proved the alteration of secondary structure of HSA in the presence of NHD. Site marker competitive experiments indicated that the binding of NHD to HSA took place in subdomain IIA region of protein. (C) 2014 Elsevier B.V. All rights reserved.