Spectroscopic Studies of the Effects of Glycation of Human Serum Albumin on L-Trp Binding

Title: Spectroscopic Studies of the Effects of Glycation of Human Serum Albumin on L-Trp Binding

Volume: 14 Issue: 1

Author(s): Abolfazl Barzegar, Ali A. Moosavi-Movahedi, Naghmeh Sattarahmady, Mohammad A. Hosseinpour-Faizi, Mohammad Aminbakhsh, Faizan Ahmad, Ali A. Saboury, Mohammad R. Ganjali and Parviz Norouzi

Affiliation:

Keywords: Conformational change, Glycation, HSA, L-Trp binding

Abstract: Modification of proteins by nonenzymatic glycation is one of the underlying factors that contribute to the development of the complications of diabetes. Human serum albumin (HSA) is one of the major targets of interaction with glucose through the Maillard reaction. The effects of 1 and 5 mg/ml glucose concentrations, which are consistent with blood glucose levels found in diabetic patients, on human serum albumin were studied by circular dichroism and fluorescence spectroscopy in sodium phosphate buffer, pH 7.4. Partial denaturation and changes in the structural integrity of HSA are caused by glycation at lower (1 mg/ml) and higher (5 mg/ml) concentrations of glucose. To study the relationship between structure and function, we investigated the interaction of L-tryptophan (L-Trp) with glycated and nonglycated HSA. The results showed that L-Trp, as the only free amino acid that substantially binds to HSA, has a lower affinity for the glycated form (especially at low concentrations of glucose) than for non-glycated HSA.

Cite this article as:

Barzegar Abolfazl, Moosavi-Movahedi A. Ali, Sattarahmady Naghmeh, Hosseinpour-Faizi A. Mohammad, Aminbakhsh Mohammad, Ahmad Faizan, Saboury A. Ali, Ganjali R. Mohammad and Norouzi Parviz, Spectroscopic Studies of the Effects of Glycation of Human Serum Albumin on L-Trp Binding, Protein & Peptide Letters 2007; 14 (1) . https://dx.doi.org/10.2174/092986607779117191