期刊
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY A-CHEMISTRY
卷 208, 期 2-3, 页码 91-96出版社
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotochem.2009.08.009
关键词
Porphyrins; Fluorescence; Singlet excited state; Host-guest interactions; PDT
资金
- Monticello College Foundation
- Iowa College Foundation
The efficacy of porphyrin binding to human serum albumin (HSA) is critical to clinical use in photodynamic therapy (PDT). Several porphyrins were utilized to measure the effect of porphyrin structure on its binding to HSA. Two categories of porphyrins were utilized: porphyrins with a hydrophobic and hydrophilic side: Protoporphyrin IX (PPIX), Protoporphyrin IX dimethylester (PPIXDE), and Chlorin er, (Ce6) and porphyrins with hydrophilic substituents on both sides: Hematoporphyrin IX (Hme), Hematoporphyrin IX dimethylester (HmeDE), and Deuteroporphyrin IX dimethylester (DPIXEG). The following methods were used for the analysis: Stern-Volmer quenching, fluorescence lifetimes, anisotropy, fluorescence binding, and homogeneous studies. The results indicate that PPIX, PPIXDE, and Ce6 bind to HSA efficiently, evidence that porphyrins bind strongly to HSA if they have a hydrophobic and hydrophilic side. Hme is thought to bind to HSA but likely to a lesser degree than the aforementioned three porphyrins. HmeDE and DPIXEG seem not to bind to HSA probably due to the lack of hydrophobic substituents. (C) 2009 Elsevier B.V. All rights reserved.
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