Abstract
We analyzed the spectral characteristics of the complexes of Zn2+, Ni2+, and Pd2+ derivatives of purpurin-18 with human serum albumin (HSA) in aqueous buffer at pH 7.0. Pd2+ in the coordination sphere of purpurin-18 decreased the affinity to HSA compared to the respective complexes of zinc and nickel derivatives. Since the formation of complexes with HSA is an important parameter of photodynamic activity of tetrapyrrolic compounds, the differential affinity of metal derivatives of purpurin-18 to this protein should be considered for the optimization of photosensitizers.
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