کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1988021 | 1540330 | 2006 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Binding of all-trans retinoic acid to human serum albumin: Fluorescence, FT-IR and circular dichroism studies Binding of all-trans retinoic acid to human serum albumin: Fluorescence, FT-IR and circular dichroism studies](/preview/png/1988021.png)
All-trans retinoic acid derived from vitamin A is an essential component for the modulation of angiogenesis, the process of blood vessel formation. We have investigated the binding of all-trans retinoic acid to the carrier protein, human serum albumin (HSA) under physiological conditions. Fluorescence quenching methods in combination with Fourier transform infrared (FT-IR) spectroscopy and circular dichroism (CD) spectroscopy were used for the biophysical studies. The binding parameters were determined by a Scatchard plot and the results found to be consistent with those obtained from a modified Stern–Volmer equation. From the thermodynamic parameters calculated according to the van’t Hoff equation, the enthalpy change ΔH0 and entropy change ΔS0 are found to be 106.17 and 106.14 J/mol K, respectively. These values suggest that apart from hydrophobic interactions electrostatic interactions are present. Changes in the CD spectra and FT-IR spectra were observed upon ligand binding along with a significant degree of tryptophan fluorescence quenching on complex formation. Docking studies performed substantiated our experimental findings and it was observed that all-trans retinoic acid hydrogen bonded with Trp 214 and Asp 451 residues of subdomain IIA and IIIA of HSA, respectively.
Journal: International Journal of Biological Macromolecules - Volume 38, Issues 3–5, 30 May 2006, Pages 197–202