Effect of chemical chaperones on glucose-induced lysozyme modifications

Bathaie, S.Z. and Nobakht, F. and Mirmiranpour, H. and Jafarnejad, A. and Moosavi-Nejad, S.Z. (2011) Effect of chemical chaperones on glucose-induced lysozyme modifications. Protein Journal, 30 (7). pp. 480-489.

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Nonenzymatic glycation of biomacromolecules occurs due to the diabetes mellitus and ageing. A number of small molecules, known as chemical chaperones, stabilize protein conformation against thermal and chemically induced denaturation. These compounds are including: polyamines (e.g. spermine and spermidine), amino acids (e.g. lysine) and polyols (e.g. glycerol). In this study the effect of spermidine (Spd), spermine (Spm), and glycerol on glycation, structure and function of lysozyme (LZ), as an extra-cellular protein, by different techniques is investigated. LZ is incubated with or without glucose (50 or 100 mM) in the absence or presence of Spd/Spm/glycerol at 37 °C up to 16 weeks. All the observed changes of glycated-LZ in comparison with the native protein, including: increased fluorescence emission, alteration in the secondary and tertiary structure, and reduced electrophoretic mobility- indicate its structural changes that are accompanied with its reduced activity. Glucose in the presence or absence of Spd induces the protein dimerization, but glucose plus Spm induces its trimmerization. In contrast, glycerol inhibits the LZ glycation and prevents the large changes on its structure and function. Glucose binds lysine residues, decreases the protein positive charges and induces some alterations in its structure and activity. Polyamines also directly bind to LZ, increase its positive charges and hence induce more glycation; more conformational changes, oligomerization and its inactivation in the presence of glucose, but glycerol affect the protein environment and preserve protein from these harmful effects. © 2011 Springer Science+Business Media, LLC.

Item Type: Article
Additional Information: cited By 7
Uncontrolled Keywords: chaperone; glucose; glycerol; lysozyme; polyamine; spermidine; spermine, article; dimerization; enzyme modification; fluorescence; glycation; protein binding; protein conformation; protein function; protein structure, Animals; Chickens; Dimerization; Glucose; Glycosylation; Molecular Chaperones; Muramidase; Protein Binding; Protein Conformation; Spermidine; Spermine
Subjects: Biochemistry, Genetics and Molecular Biology
Divisions: Faculty of Medicine > Basic Sciences > Department of Biochemistry
Depositing User: editor . 2
Date Deposited: 27 Feb 2017 09:31
Last Modified: 11 Mar 2017 14:36
URI: http://eprints.kaums.ac.ir/id/eprint/834

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