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The interaction of dansyl amino acids with bovine serum albumin

  • Colloid Science
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Abstract

The interaction of 5-dimethylaminonaphthalene-1-sulfonyl (DNS or dansyl) amino acids with bovine serum albumin (BSA) was investigated by means of fluorescence measurements. Fluorometric titrations revealed that BSA has one high affinity site (binding constant,K a=105∼106 M−1), and other sites of lower affinity (K a=103∼104 M−1) for the probes. Static excitation and emission spectra, lifetimes, time resolved emission spectra, and anisotropy data indicated that the binding is stabilized mainly through fixation by the high affinity binding site. The binding constant significantly decreased with the increase of the spacer distance between the dansyl and anionic groups of the probe molecule. This observation was explained by considering the change of the electrostatic interaction between the anionic group of the probe and a cationic residue in the vicinity of the site.

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Author notes

  1. T. Iijima

    Present address: Department of Polymer Science, Tokyo Institute of Technology, Ookayama, Megro-ku, 152, Tokyo, Japan

Authors and Affiliations

  1. Department of Polymer Science, Tokyo Institute of Technology, Ookayama, Megro-ku, 152, Tokyo, Japan

    T. Seki & J. Komiyama

  2. Physical Chemistry Laboratory, Swiss Federal Institute of Technology, CH-8092, Zurich, Switzerland

    U. P. Wild

Authors
  1. T. Seki
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  2. J. Komiyama
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  3. T. Iijima
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  4. U. P. Wild
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Seki, T., Komiyama, J., Iijima, T. et al. The interaction of dansyl amino acids with bovine serum albumin. Colloid & Polymer Sci 262, 311–318 (1984). https://doi.org/10.1007/BF01410470

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  • DOI: https://doi.org/10.1007/BF01410470

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