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.
School of Chemistry and Chemical Engineering, Guangdong Pharmaceutical University, Guangzhou, PR China. zhaoping666@163.com
Ping
P
Zhao
Jin-Wang
JW
Huang
Liang-Nian
LN
Ji
D000042:Absorption; D000818:Animals; D002412:Cations; D002417:Cattle; D002942:Circular Dichroism; D004583:Electrons; D006863:Hydrogen-Ion Concentration; D011166:Porphyrins / Q000737:chemistry / Q000378:metabolism*; D011726:Pyridinium Compounds / Q000737:chemistry / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013059:Spectrum Analysis, Raman; D013499:Surface Properties; D017186:Titrimetry
D002412:Cations; D011166:Porphyrins; D011726:Pyridinium Compounds; D012710:Serum Albumin, Bovine