Maiti, Tushar Kanti ; Ghosh, Kalyan Sundar ; Debnath, Joy ; Dasgupta, Swagata (2006) Binding of all-trans retinoic acid to human serum albumin: fluorescence, FT-IR and circular dichroism studies International Journal of Biological Macromolecules, 38 (3-5). pp. 197-202. ISSN 0141-8130
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Official URL: https://www.sciencedirect.com/science/article/pii/...
Related URL: http://dx.doi.org/10.1016/j.ijbiomac.2006.02.015
Abstract
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.
Item Type: | Article |
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Source: | Copyright of this article belongs to Elsevier Science. |
Keywords: | All-Trans RA; Human Serum Albumin; Fluorescence Studies; FT-IR And CD Studies; Docking |
ID Code: | 113758 |
Deposited On: | 15 May 2018 11:30 |
Last Modified: | 15 May 2018 11:30 |
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