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Hematoporphyrin diethers--V. Plasma protein binding and photosensitizing efficiency
M Kongshaug1, C Rimington, J F Evensen
1Department of Biophysics, Norwegian Radium Hospital, Oslo.
The International Journal of Biochemistry
|January 1, 1990
Summary
Hematoporphyrin (HP) ethers bind to human plasma proteins and low-density lipoproteins (LDL). This binding correlates with tumor growth delay and polarity, except for one HP ether, suggesting specific interactions for photosensitizing applications.
Area of Science:
- Biochemistry
- Photochemistry
- Oncology
Background:
- Hematoporphyrin (HP) derivatives are investigated for photodynamic therapy.
- Understanding the binding of HP ethers to plasma proteins and lipoproteins is crucial for their therapeutic efficacy.
Purpose of the Study:
- To investigate the binding of hematoporphyrin (HP) ethers to human plasma proteins and lipoproteins.
- To correlate LDL binding with photosensitized tumor growth delay and polarity.
Main Methods:
- Ultracentrifugation was used to study the binding of HP ethers to plasma proteins and lipoproteins.
- High-Performance Liquid Chromatography (HPLC) was employed to determine the degree of polarity.
Main Results:
- A uniform relationship was observed between LDL binding, photosensitizing efficiency, and polarity for most HP ethers.
- HP-diamyl ether was an exception, showing a different binding profile.
- Less related dyes like HP, tetraphenylporphyrin tetrasulfonate, and HP-dimethyl ether did not exhibit this uniform relationship.
Conclusions:
- The binding of HP ethers to LDL is a key factor influencing their photosensitizing efficiency and polarity.
- Specific structural features of HP ethers, like HP-diamyl ether, can alter these interactions.
- These findings have implications for optimizing HP-based photosensitizers in cancer treatment.