Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5399431 | Journal of Luminescence | 2014 | 7 Pages |
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 2.79Ã104Â Mâ1 at 298.15Â 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 (ÎH=â29.22Â kJÂ molâ1 and ÎS=â12.91Â JÂ molâ1Â Kâ1), 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.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Physical and Theoretical Chemistry
Authors
Bahar Kancı BozoÄlan, Sibel Tunç, Osman Duman,