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Oxidative Damage of Lysozyme and Human Serum Albumin and Their Mixtures. A Comparison of Photosensitized and Peroxyl Radical Promoted Processes

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Abstract

Oxidative modifications of lysozyme (Lyso) and human serum albumin (HSA) mediated by photoinduced processes and peroxyl radicals were studied. Both oxidative conditions were applied to the separate proteins and their mixtures. Dimerization and fragmentation of the proteins do not correlate with the formation of carbonyls or peroxides, implying that evaluation of these changes is not an index of the overall oxidative modification of a protein. The results obtained also show that the hypothesis that the electrostatic interactions of Lyso and HSA could facilitate the formation of Lyso-HSA dimers in the presence of a source of reactive oxygen species was verified in both ROS-producing systems.

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Abbreviations

HSA:

Human serum albumin

Lyso:

Lysozyme

RF:

Riboflavin

MB:

Methylene blue

AAPH:

2,2′-azobis(2-amidinopropane) dihydrochloride

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Acknowledgments

This work was supported by Proyecto Puente 05/2009 and FONDECYT (Grant 1070285).

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Authors and Affiliations

  1. Departamento de Química Física, Facultad de Química, Pontificia Universidad Católica de Chile, C.P. 782 0436, Santiago, Chile

    Andrea Arenas, Rodrigo Vasquez & Eduardo Silva

  2. Departamento de Farmacia, Facultad de Química, Pontificia Universidad Católica de Chile, Santiago, Chile

    Camilo López-Alarcón

  3. Facultad de Química y Biología, Universidad de Santiago de Chile, Santiago, Chile

    Eduardo Lissi

Authors
  1. Andrea Arenas
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  2. Rodrigo Vasquez
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  3. Camilo López-Alarcón
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  4. Eduardo Lissi
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  5. Eduardo Silva
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Corresponding author

Correspondence to Eduardo Silva.

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Arenas, A., Vasquez, R., López-Alarcón, C. et al. Oxidative Damage of Lysozyme and Human Serum Albumin and Their Mixtures. A Comparison of Photosensitized and Peroxyl Radical Promoted Processes. Protein J 30, 359–365 (2011). https://doi.org/10.1007/s10930-011-9341-1

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  • DOI: https://doi.org/10.1007/s10930-011-9341-1

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