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DETERMINANTS OF PHOTOSENSITIZATION BY MONO‐L‐ASPARTYL CHLORIN e6
Author(s) -
KESSEL DAVID
Publication year - 1989
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1989.tb09193.x
Subject(s) - chlorin , chemistry , photosensitizer , photodynamic therapy , mace , fluorescence , biophysics , biochemistry , photochemistry , cytoplasm , membrane , porphyrin , in vitro , biology , organic chemistry , psychology , physics , quantum mechanics , psychiatry , myocardial infarction , conventional pci
— The mono‐N‐aspartyl derivative of chlorin e6 (MACE) is a new photosensitizer being examined for use in antineoplastic photodynamic therapy. Studies were carried out to identify unique aspects of MACE localization by murine leukemia L1210 cells in vitro. Octanol/water partitioning studies were used to quantitate the hydrophobicity of MACE and two analogs, chlorin e6 and mesochlorin. Sites of cellular localization of these dyes were probed by fluorescence studies, and by examining loci of photodamage. These studies indicate that MACE, a hydrophilic dye, partitions to cytoplasmic loci. Data obtained with chlorin e6, a more hydrophobic dye, are consistent with binding at both membrane and cytoplasmic sites. A substantially more hydrophobic product, meso‐chlorin, binds primarily to the cell membrane. While the tumor‐localizing porphyrin product HPD binds to plasma LDL < HDL. MACE and CE are predominantly bound to plasma protein and HDL. Patterns of distribution and localization of MACE differ substantially from those observed with HPD and other hydrophobic sensitizers. Phototoxic effects of MACE could not be specifically attributed to membrane or mitochondrial damage.