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Photosensitization of small peptides by proflavine: An E.S.R. study at low temperature

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Summary

The photosensitization by proflavine of dipeptides containing glycine and histidine, methionme, tryptophan or tyrosine is studied by ESR spectroscopy at 77 °K. It is shown that the induced free radicals are never localized in glycine but for a large part in the other constituent ammo-acid. Furthermore, and in contradiction with the conclusions reached by other physico-chemical techniques, experimental evidences are presented hi favor of the induction of a free radical associated with the breakage of the peptide bond.

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Authors and Affiliations

  1. Department of Atomic and Molecular Physics, Institute of Physics, University of Liège, B-4000, Sart-Tilman par Liège 1, Belgium

    Yves Lion &  Albert van de Vorst

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  1. Yves Lion
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  2. Albert van de Vorst
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Lion, Y., van de Vorst, A. Photosensitization of small peptides by proflavine: An E.S.R. study at low temperature. Radiat Environ Biophys 11, 239–245 (1974). https://doi.org/10.1007/BF01323193

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  • DOI: https://doi.org/10.1007/BF01323193

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