Spectroscopic and computational exploration of hypoxanthine riboside interacting with plasma albumin

Abstract

Hypoxanthine riboside (HXR) is a nucleoside essential for wobble base pairs to translate the genetic code. In this work, an absorption and luminescence study showed that HXR and human serum albumin (HSA) formed a new complex through hydrogen bonds and van der Waals forces at ground state. Fluorescence probe experiments indicated that HXR entered the first subdomain of domain II in HSA and was fixed by amino acid residues in site I defined by Sudlow, and after competing with a known site marker. The recognition interaction featured negative ΔH ϴ , ΔS ϴ and ΔG ϴ thermodynamic parameters. Fluorescence and circular dichroism spectra described the polarity of residues and α-helix and β-strand content changed because of HXR binding. The most rational structure for the HXR-HSA complex was recommended by the molecular docking method, in which the binding location, molecular orientation, adjacent amino acid residues, and hydrogen bonds were included. In addition, the influence of β-cyclodextrin and some essential metal ions on the balance of the HSA-HXR system interaction was measured. The study gained comprehensive information on the transportation mechanism for HXR in blood, and was of great significance in understanding the theory of HXR biotransformation and in discussing its clinical in vivo half-life.

Spectroscopic and computational studies on the binding interaction between gallic acid and Pin1

“…Circular dichroism is one of the most effective techniques for studying the secondary structural changes of protein–ligand systems. To quantitatively calculate the α‐helix content, the following equations were used [ 39 ] : where MRE 208 is mean residue elliptically (MRE) at 208 nm, and C p , n and l are the molar concentration of Pin1 (10 μmol/L), the number of amino acid residues (163) and the path length of the cell (0.1 cm), respectively.…”