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Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/jspui/handle/10054/9683

Title: Spectral investigations of the interaction of some porphyrins with bovine serum albumin
Authors: CHATTERJEE, S
SRIVASTAVA, TS
Keywords: water-soluble porphyrins
vivo photosensitizing efficacy
photodynamic therapy
tumor photosensitizers
rose-bengal
binding
dna
metalloporphyrins
fluorescence
mitochondria
Issue Date: 2000
Publisher: JOHN WILEY & SONS LTD
Citation: JOURNAL OF PORPHYRINS AND PHTHALOCYANINES, 4(2), 147-157
Abstract: The binding of meso-tetrakis[4-(carboxymethyleneoxy)phenyl]porphyrin (T4CPP), meso-tetrakis[3-(carboxymethyleneoxy)phenyl]porphyrin (T3CPP) and meso-tetrakis[3,4-bis(carboxymethyl eneoxy)phenyl]porphyrin (T3, 4BCPP) with bovine serum albumin (BSA) at pH 7.4 has been studied at 420 nm in detail. The results show hypochromicity along with a red shift in the Soret band of the porphyrins, This suggests that these porphyrins bind to BSA as monomers. Further analysis of these data supports the noninteractive binding of T4CPP and T3CPP with BSA and the cooperative binding of T3, 4BCPP with BSA. These binding data have been interpreted in terms of one specific binding site and several non-specific binding sites on BSA for the porphyrins. The absorption spectral changes of the porphyrins between 400 and 450 nm when titrated with BSA suggest that there is another specific binding site on BSA for the porphyrins, These two specific binding sites have also been supported by circular dichroism (CD) studies. The absorption spectral and CD studies on the interactions of the porphyrins with BSA further suggest that these interactions are dependent on the number and configuration of substituents in the phenyl groups of the porphyrins. The contact energy transfer from the aromatic amino acid residues tryptophan and tyrosine of BSA to the porphyrins in the BSA-porphyrin complexes has also been studied using fluorescence spectroscopy. These energy transfer data show the energy transfer from tryptophan to the porphyrins for their binding to site I of BSA and from tyrosine to the porphyrins for their binding to site II of BSA, Unfolding studies of the BSA-porphyrin systems indicate that the tertiary structure is essential for the binding of the porphyrins. A correlation between the accumulation of Tc-99m-labelled T4CPP and T3, 4BCPP in tumour tissue and their binding at site II of BSA is possible. The interaction of the porphyrins can also be used as a model for mitochondrial interactions. Copyright (C) 2000 , Ltd.
URI: http://dx.doi.org/10.1002/(SICI)1099-1409(200003)4:2<147::AID-JPP163>3.0.CO;2-Z
http://dspace.library.iitb.ac.in/xmlui/handle/10054/9683
http://hdl.handle.net/10054/9683
ISSN: 1088-4246
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