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Effect of Chemical Chaperones on Glucose-Induced Lysozyme Modifications

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Abstract

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.

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Abbreviations

Glc:

Glucose

LZ:

Lysozyme

Spm:

Spermine

Spd:

Spermidine

AGE:

Advanced glycation endproducts

CD:

Circular dichroism

Asp:

Aspartate

Glu:

Glutamate

Arg:

l-Arginine

Lys:

l-Lysine

AG:

Aminoguanidine

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Acknowledgments

This research was supported by Iranian National Science Foundation grant No. 88000429. The authors are also very thankful to the Research Council of Tarbiat Modares University for supporting this project.

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Authors and Affiliations

  1. Department of Clinical Biochemistry, Faculty of Medical Sciences, Tarbiat Modares University, P.O. Box: 14115-111, Tehran, Iran

    S. Zahra Bathaie & B. B. Fateme Nobakht

  2. Department of Biochemistry, Faculty of Medicine, Tehran University of Medical Sciences, Tehran, Iran

    Hossein Mirmiranpour

  3. Faculty of Medicine, Kashan Medical Sciences University, Kashan, Iran

    Akbar Jafarnejad

  4. Department of Biochemistry, Alzahra University, Tehran, Iran

    S. Zahra Moosavi-Nejad

Authors
  1. S. Zahra Bathaie
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  2. B. B. Fateme Nobakht
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  3. Hossein Mirmiranpour
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  4. Akbar Jafarnejad
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  5. S. Zahra Moosavi-Nejad
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Correspondence to S. Zahra Bathaie.

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Bathaie, S.Z., Nobakht, B.B.F., Mirmiranpour, H. et al. Effect of Chemical Chaperones on Glucose-Induced Lysozyme Modifications. Protein J 30, 480–489 (2011). https://doi.org/10.1007/s10930-011-9353-x

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