Generic placeholder image

Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

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

Volume 14, Issue 1, 2007

Page: [13 - 18] Pages: 6

DOI: 10.2174/092986607779117191

Price: $65

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.

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


Rights & Permissions Print Export Cite as
© 2022 Bentham Science Publishers | Privacy Policy