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The effect of porphyrin structure on binding to human serum albumin by fluorescence spectroscopy

Paper ID Volume ID Publish Year Pages File Format Full-Text
27813 44044 2009 6 PDF Available
Title
The effect of porphyrin structure on binding to human serum albumin by fluorescence spectroscopy
Abstract

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 e6 (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.

Keywords
Porphyrins; Fluorescence; Singlet excited state; Host–guest interactions; PDT
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The effect of porphyrin structure on binding to human serum albumin by fluorescence spectroscopy
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology A: Chemistry - Volume 208, Issues 2–3, 15 December 2009, Pages 91–96
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Price was $35.95
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