Examination of Protein-Damaging Activity of Phosphorus(V) Porphyrin Photosensitizer for Photodynamic Therapy | OMICS International | Abstract
ISSN: 2155-9872

Journal of Analytical & Bioanalytical Techniques
Open Access

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Research Article

Examination of Protein-Damaging Activity of Phosphorus(V) Porphyrin Photosensitizer for Photodynamic Therapy

Kazutaka Hirakawa1*, Taiki Yamanaka1 , Jin Matsumoto2 and Masahide Yasuda2

1Department of Applied Chemistry and Biochemical Engineering, Graduate School of Engineering, Shizuoka University, Japan

2Department of Applied Chemistry, Faculty of Engineering, University of Miyazaki, Japan

*Corresponding Author:
Kazutaka Hirakawa
Department of Applied Chemistry and Biochemical Engineering
Graduate School of Engineering
Shizuoka University, Johoku 3-5-1
Naka-ku, Hamamatsu, Shizuoka 432-8561, Japan
Tel: +81-53-478-1287
Fax: +81-53-478-1287
E-mail: [email protected]

Received date: April 27, 2013; Accepted date: May 29, 2013; Published date: May 31, 2013

Citation: Hirakawa K, Yamanaka T, Matsumoto J, Yasuda M (2013) Examination of Protein-Damaging Activity of Phosphorus (V) Porphyrin Photosensitizer for Photodynamic Therapy. J Anal Bioanal Tech S1:003. doi: 10.4172/2155-9872.S1-003

Copyright: © 2013 Menon D. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


For the fundamental study of photodynamic therapy, protein-damaging activity of the water-soluble phosphorus(V) porphyrin (DDP(V)TPP) was examined. Absorption spectrum measurement demonstrated the binding interaction between DDP(V)TPP and human serum albumin, a water-soluble protein. Photo-irradiated DDP(V)TPP damaged the amino acid residue of human serum albumin, resulting in the decrease of fluorescence intensity from the tryptophan residue of human serum albumin. Protein damage photosensitized by DDP(V)TPP was inhibited by the addition of sodium azide and enhanced in deuterium oxide, indicating the contribution of singlet oxygen. However, sodium azide could not completely inhibit the damage of human serum albumin, suggesting that the electron transfer mechanism contributes to protein damage as does singlet oxygen generation. Isolated tryptophan was also damaged by a photosensitization of DDP(V)TPP in solution, whereas DDP(V)TPP did not induce photodamage to tyrosine and phenylalanine. Using the application of a fluorometry of hydrogen peroxide, the deactivation of catalase photosensitized by DDP(V)TPP was demonstrated.