Article ID Journal Published Year Pages File Type
5401518 Journal of Luminescence 2012 6 Pages PDF
Abstract
► Interactions between dfppip and BSA were investigated by fluorescence quenching. ► Quenching mechanism mainly arise from the formation of BSA-imidazole complex. ► D→A distance is <8 nm indicates that the energy transfer from BSA to dfppip. ► Synchronous fluorescence spectra to exploit the structural change of BSA. ► Effect of other ions on the binding constants between dfppip and BSA.
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Related Topics
Physical Sciences and Engineering Chemistry Physical and Theoretical Chemistry
Preview
A study on the binding interaction between the imidazole derivative and bovine serum albumin by fluorescence spectroscopy
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