Cationic pyridinium porphyrins appending different peripheral substituents: Spectroscopic studies on their interactions with bovine serum albumin

The interaction of cationic pyridinium porphyrins appending methylpyridyl, hydroxyphenyl, propionoxyphenyl or carboxyphenyl group at meso-20-position of porphyrin core with bovine serum albumin (BSA), was studied by the combination of absorption spectroscopy, surface-enhanced Raman spectroscopy (SERS), circular dichroism (CD) spectroscopy, fluorescence spectroscopy and synchronous spectroscopy. The spectral monitoring results indicate that the studied compounds could bind with the BSA molecule and the calculated binding constants show that the tetracationic porphyrin has higher binding affinity than those tricationic ones. The interactions between porphyrins and BSA employ an electrostatic binding mechanism and there was only one binding site which located on the surface of the protein molecule.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► There was one binding site between porphyrin and BSA, which located on the surface of BSA. ► Tetracationic porphyrin has higher binding affinity to BSA than tricationic ones. ► Surface-enhanced Raman spectroscopy was firstly employed in this research area.