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Effect of increased hydrophobicity on the binding of two model amphiphilic chlorin drugs for photodynamic therapy with blood plasma and its components.

Abstract
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.
AuthorsPadmaja P Mishra, Sunita Patel, Anindya Datta
JournalThe journal of physical chemistry. B (J Phys Chem B) Vol. 110 Issue 42 Pg. 21238-44 (Oct 26 2006) ISSN: 1520-6106 [Print] United States
PMID17048951 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Drug Carriers
  • Lipoproteins
  • Photosensitizing Agents
  • Porphyrins
  • Serum Albumin
  • chlorin p6
  • purpurin 18
  • chlorin
Topics
  • Drug Carriers (chemistry)
  • Hydrophobic and Hydrophilic Interactions
  • Lipoproteins (metabolism)
  • Photochemotherapy
  • Photosensitizing Agents (administration & dosage, chemistry, pharmacology)
  • Plasma
  • Porphyrins (administration & dosage, chemistry, pharmacokinetics)
  • Protein Binding
  • Serum Albumin (metabolism)

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