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Evidence for covalent binding of epicocconone with proteins from synchronous fluorescence spectra and fluorescence lifetimes

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Abstract

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 ground-state 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 N-terminus of the protein.

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Authors and Affiliations

  1. Department of Chemistry, Indian Institute of Technology — Bombay, Powai, Mumbai, 400 076, India

    Debashis Panda & Anindya Datta

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  1. Debashis Panda
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  2. Anindya Datta
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Correspondence to Anindya Datta.

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Panda, D., Datta, A. Evidence for covalent binding of epicocconone with proteins from synchronous fluorescence spectra and fluorescence lifetimes. J Chem Sci 119, 99–104 (2007). https://doi.org/10.1007/s12039-007-0016-6

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  • DOI: https://doi.org/10.1007/s12039-007-0016-6

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