chlorin-p6 has been researched along with purpurin-18* in 2 studies
2 other study(ies) available for chlorin-p6 and purpurin-18
| Article | Year |
|---|---|
Steady state and time-resolved fluorescence investigation of the specific binding of two chlorin derivatives with human serum albumin.
The specific binding of two model drugs for photodynamic therapy, namely chlorin p6 and purpurin 18 in the vicinity of Sudlow's Site I of HSA has been investigated by monitoring the intrinsic fluorescence of single tryptophanyl residue and by competitive binding with warfarin. The distance from the tryptophanyl residue has been ascertained by FRET from Trp to the chlorins and has been found to indicate a binding to Sudlow's Site I. The principal driving force for the interaction is found to be the hydrophobic effect. The main mechanism of protein fluorescence quenching was static. Time-resolved fluorescence results of competitive binding with warfarin are found to confirm that they bind to the warfarin binding site. Topics: Binding, Competitive; Circular Dichroism; Fluorescence Resonance Energy Transfer; Humans; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Photosensitizing Agents; Porphyrins; Protein Binding; Serum Albumin; Thermodynamics; Tryptophan; Warfarin | 2007 |
Effect of increased hydrophobicity on the binding of two model amphiphilic chlorin drugs for photodynamic therapy with blood plasma and its components.
The binding of serum albumin and lipoprotein with chlorin p(6) and purpurin 18, two structurally related chlorins, has been studied to understand the role for these proteins as endogenous carriers for these drugs. As a drug carrier a protein may aid in selective delivery of a drug to a tumor region. Binding with serum albumin may result in accumulation of the drug in the stroma of the tumor cell and lead to a reduction of cellular uptake of photosensitizers. However, it is possible that this factor may not be a problem for cellular uptake of chlorin p(6) and purpurin 18 by the tumor tissues, since it binds more efficiently with low-density lipoprotein when it become more lipophilic, indicating that the principal carriers for these molecules are lipoproteins. Since the tumor tissues contain numerous lipoprotein receptors, chlorin p(6) and purpurin 18 could be internalized more efficiently in tumor cells. Topics: Drug Carriers; Hydrophobic and Hydrophilic Interactions; Lipoproteins; Photochemotherapy; Photosensitizing Agents; Plasma; Porphyrins; Protein Binding; Serum Albumin | 2006 |