Determination of Amadori Product in Glycated Human Serum Albumin by Spectroscopy Methods

Abstract

The Amadori product is a stable intermediate in the glycation process, and its increased formation is a marker of hyperglycemia in diabetes mellitus. Its accumulation in the body contributes to pathological complications of diabetes including diabetic nephropathy and retinopathy, and cardiovascular diseases. In this study the effect of 3‐β‐hydroxybutyrate on the production of Amadori products and structural changes of human serum albumin (HSA) after incubation with glucose was investigated using FT‐IR, circular dichroism (CD), and UV‐visible and fluorescence spectroscopy. Our results showed that the production of Amadori products in HSA incubated with glucose was decreased in the presence of 3‐β‐hydroxybutyrate. The glycation‐mediated alterations in HSA secondary and tertiary structures were also reduced in the presence of 3‐β‐hydroxybutyrate. These changes were attributed to reduced formation of glucose covalent bonds with the HSA lysine residues in the presence of 3‐β‐hydroxybutyrate. Thus, 3‐β‐hydroxybutyrate reduced the production of Amadori products by reacting with lysine residues and decreasing HSA covalent modifications by glucose.

Structural and Dynamic Alteration of Glycated Human Serum Albumin in Schiff Base and Amadori Adducts: A Molecular Simulation Study

“…Compared to native HSA, the denaturation of the protein structure is identified in both cases (Table ). This structure decomposition is in good agreement with the previous experimental studies. , Approximately ∼10% helicity is lost in SCH and AMA. These regions seem to mostly decompose into turns (Table ).…”

“…This structure decomposition is in good agreement with the previous experimental studies. 44,45 Approximately ∼10% helicity is lost in SCH and AMA. These regions seem to mostly decompose into turns (Table 1).…”

Quantification and Improvement of the Dynamics of Human Serum Albumin and Glycated Human Serum Albumin with Astaxanthin/Astaxanthin-Metal Ion Complexes: Physico-Chemical and Computational Approaches

“…Comparing the spectra of HSA and gHSA, an increase in absorbance was observed for the latter. The increase in the absorbance peak of gHSA was attributed to the change in the secondary structure of the protein due to the formation of Amadori product occurring between glycation agents with the HSA lysines [19]. In Figure 1B, the UV-Vis spectra of ASX dissolved in EtOH at different concentrations, with the absorbance peak at 486 nm, is reported.…”