Binding of all-trans retinoic acid to human serum albumin: fluorescence, FT-IR and circular dichroism studies.
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Maiti TK, Ghosh KS, Debnath J, Dasgupta S
Binding of all-trans retinoic acid to human serum albumin: fluorescence, FT-IR and circular dichroism studies.
Int J Biol Macromol. 2006 May 30;38(3-5):197-202. Epub 2006 Mar 6.
- PubMed ID
- 16569428 [ View in PubMed]
- 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 DeltaH(0) and entropy change DeltaS(0) are found to be 106.17 and 106.14J/molK, 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.
DrugBank Data that Cites this Article
- Drug Carriers
Drug Carrier Kind Organism Pharmacological Action Actions Tretinoin Serum albumin Protein Humans UnknownBinderDetails