The effect of human serum albumin glycation on the binding of antidiabetic agent-exenatide; the multispectroscopic studies. Part II

Abstract

The glycated human serum albumin (gHSA) interaction with antidiabetic agent – exenatide (exe) was investigated by spectroscopic techniques. The fluorescence spectroscopy showed an association between exe and protein as 4.57 × 104 M−1 (290 K), 3.33 × 104 M−1 (300K) and 2.54 × 104 M−1 (310K) and the number of binding sites were 1.15, 1.09, and 1.02, respectively. The binding process occurred spontaneously and the electrostatic bonds play a predominant role in the gHSA-exe interaction. The affinity drug to gHSA was studied in the presence of metal ions (Ca2+, Cr3+, Zn2+), which are often given as a supplement to the diet. Our study indicates that metal ions have an effect on the increase of the affinity of exenatide to glycated albumin and it is the result of the metal ion-exenatide-albumin interaction. Based on CD spectroscopy it is evident that exenatide has nonsignificant effect on the protein secondary structure, but the changes are visible in the presence of metal ions. Zeta potential measurements indicate instability of the system at lower concentration of the ligand - the effect is desired in point of view of pharmacology.