The interactions between bovine serum albumin (BSA) and two Cu(II) phenanthroline complexes were studied by fluorescence and UV-visible absorption spectroscopy. The obtained results confirm that the phen ligand (phen = 1,10-phenanthroline) is dissociated from the two complexes and moves into the hydrophobic cavity of BSA and that the M–L complexes (M = Co2+, Cu2+; L = Hlact, imda; Hlact = lactic acid, H2imda = iminodiacetic acid) coordinate with the amino acids on the surface of the peptide in the solution. This mode of action significantly inhibits the denaturation of BSA. The calculated distance between the BSA and the two complexes suggests that the energy transfer from the excited state of BSA to a complex occurs with high efficiency.
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Abstract of article is published in Zhurnal Prikladnoi Spektroskopii, Vol. 84, No. 1, p. 169, January–February, 2017.
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Lin, HB., Shen, QH. Luminescence Studies of the Ligand Exchange Between Two Phenanthroline Complexes and Bovine Serum Albumin. J Appl Spectrosc 84, 170–176 (2017). https://doi.org/10.1007/s10812-017-0446-y
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DOI: https://doi.org/10.1007/s10812-017-0446-y