Spectrofluorometric studies of the interaction of chaetochromin A with serum albumin
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The fluorescence emission of chaetochromin A was examined at various conditions and its mode of binding to serum albumin and mitochondrial membrane protein(s) was discussed. Chaetochromin A emitted fluorescence in pyridine and N, N-dimethylformamide (DMFA), and did not in ethanol and benzene. The excitation and emission wavelengths were 415 and 515nm, respectively. Chaetochromin A was not fluorescent in bufferized aqueous solution (pH 7.4). In the presence of BSA, it was fluorescent, exhibiting the pH-dependent alteration of fluore-scence intensity. The magnitude of fluorescence intensity was the largest at pH around 7.5. Chaetochromin A was not fluorescent in the presence of anionic detergent sodium dodecyl sulfate (SDS), but was eminently fluorescent in the presence of cationic detergent benzalkonium chloride (pH 7.4).
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