Physicochemical properties and stability of anthralin in model systems and human skin.
Physicochemical properties and stability of anthralin in model systems and human skin.
复制标题
蒽林在模型系统和人体皮肤中的理化性质和稳定性。
DOI:
10.1111/1523-1747.ep12530811
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发表时间:
1983
期刊:
影响因子:
--
通讯作者:
R. Santus
中科院分区:
文献类型:
--
作者:
T. S. Melo;L. Dubertret;P. Prognon;A. Gond;G. Mahuzier;R. Santus
The physico-chemical properties and the stability of anthralin, a potent antipsoriatic agent, has been investigated in model systems by optical absorption and fluorescence spectroscopy and by gas chromatography coupled to mass spectrometry. Systematic studies were carried out on anthralin and its oxidation products (1,8-dihydroxyanthraquinone and 1,8-1',8'-tetrahydroxydianthron). Anthralin and 1,8-dihydroxyanthraquinone are shown to readily bind to human serum albumin and not to DNA. Anthralin bound to albumin readily oxidizes, yielding the 1,8-dihydroxyanthraquinone which is fairly stable. These results are correlated with those obtained with intact whole human epidermis and suction blister fluid showing that, in the former case, anthralin binds to protein as suggested by absorption and fluorescence spectroscopies. Gas chromatography-mass spectrometry analysis makes it easy to detect anthralin and 1,8-dihydroxyanthraquinone in suction blister fluid doped with anthralin but not in suction blister obtained after topical application on normal human skin.