Articles written in Journal of Chemical Sciences
Volume 119 Issue 2 March 2007 pp 99-104
Synchronous fluorescence and time-resolved fluorescence spectroscopic studies that reveal the interaction of epicocconone with human serum albumin is significantly different from its interaction with surfactant assemblies. This observation, along with steady-state fluorescence data, indicates groundstate interaction between the fluorophore epicocconone and the protein. Similarity in fluorescence properties with the adduct of the fluorophore with 𝑛-butylamine indicates that bonding occurs at the Nterminus of the protein.
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