A new Phenol Red-modified porphyrin as efficient protein photocleaving agent

Literature Information

Publication Date 2010-08-16
DOI 10.1039/C0CP00012D
Impact Factor 3.676
Authors

Wan-Hua Lei, Yuan-Jun Hou, Xue-Song Wang, Bao-Wen Zhang


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Abstract

Protein affinity is of importance for porphyrins in their application in photodynamic therapy (PDT). A new Phenol Red-modified porphyrin (R-TPP) was designed and synthesized to fully take advantage of the binding character of Phenol Red towards protein. Detailed comparisons of absorption spectra, fluorescence spectra, n-octanol/water partition coefficients, 1O2 quantum yields, as well as protein photocleaving abilities between R-TPP and its parent porphyrin Br-TPP clearly demonstrate the benefits stemming from the modification of Phenol Red. On one hand, the presence of Phenol Red moiety greatly enhances the binding affinity of R-TPP towards model proteins (bovine serum albumin and hen egg lysozyme), and therefore improves the availability of 1O2. On the other hand, the presence of Phenol Red moiety provides R-TPP with amphiphilic character, and therefore restricts aggregation and favors the generation of 1O2. As a result, R-TPP photocleaves proteins efficiently, showing promising application potential in PDT.

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Physical Chemistry Chemical Physics
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