Spectroscopic studies of the effects of glycation of human serum albumin on L-Trp binding.

Spectroscopic studies of the effects of glycation of human serum albumin on L-Trp binding. Research Abstract Details 

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Spectroscopic studies of the effects of glycation of human serum albumin on L-Trp binding. Abstract Text:

Abolfazl Barzegar,Ali A Moosavi-Movahedi,Naghmeh Sattarahmady,Mohammad A Hosseinpour-Faizi,Mohammad Aminbakhsh,Faizan Ahmad,Ali A Saboury,Mohammad R Ganjali,Parviz Norouzi,

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 non-glycated 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.

Spectroscopic studies of the effects of glycation of human serum albumin on L-Trp binding. Publishing Authors By Initials

A Barzegar,AA Moosavi-Movahedi,N Sattarahmady,MA Hosseinpour-Faizi,M Aminbakhsh,F Ahmad,AA Saboury,MR Ganjali,P Norouzi,

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Spectroscopic studies of the effects of glycation of human serum albumin on L-Trp binding. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Protein and peptide letters

VOLUME: 14

Page Numbers: 13-8

Journal Abbreviation: Protein Pept. Lett.

ISSN: 0929-8665

DAY: 1

MONTH: 02

YEAR: 2007

Spectroscopic studies of the effects of glycation of human serum albumin on L-Trp binding. Information

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LANGUAGE: eng

NlmUniqueID: 9441434

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AFFILIATION: Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran. moosavi@ibb.ut.ac.ir.

Country: Netherlands

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MEDLINETA: Protein Pept Lett

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