PHOTODYNAMIC INACTIVATION OF RETROVIRUSES BY PHTHALOCYANINES - THE EFFECTS OF SULFONATION, METAL-LIGAND AND FLUORIDE

PHOTODYNAMIC INACTIVATION OF RETROVIRUSES BY PHTHALOCYANINES - THE EFFECTS OF SULFONATION, METAL-LIGAND AND FLUORIDE
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DOI:
10.1016/1011-1344(92)85053-w
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发表时间:
1992-04-30
影响因子:
5.4
通讯作者:
VANSTEVENINCK, J
VANSTEVENINCK, J
中科院分区:
生物学2区
文献类型:
--
作者:
BENHUR, E;HOEBEN, RC;VANSTEVENINCK, J

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用酞菁铝和锌衍生物研究了逆转录病毒的光动力失活。在两种小鼠细胞系Psi2和PA317中包装的N2逆转录病毒被用作包膜病毒的模型。AlPc衍生物比相应的ZnPc衍生物在光动力学上更有效地灭活病毒。Pc大环磺化逐渐降低了AlPc和ZnPc的光动力活性。光照下5 mM的氟化物完全保护病毒不被AlPc灭活。在F-存在的情况下,磺化衍生物AlPcS1和AlPcS4的失活率分别降低了2.5倍和2倍。在生物膜(红细胞鬼)中,F-对alpcs4致敏的脂质过氧化无显著影响。在类似的条件下,幽灵中幽灵单体的交联被严重抑制(E. Ben-Hur and A. Orenstein, Int.)。j . Radiat。医学杂志。, 60(1991) 293-301)。由于Pc衍生物不能灭活非包膜病毒,因此假设通过光动力损伤包膜蛋白发生灭活。磺酸残基的取代减少了Pc衍生物与包膜蛋白的结合,从而降低了它们的光动力功效和F-修饰它的能力。
The photodynamic inactivation of retroviruses was investigated using aluminium and zinc phthalocyanine (Pc) derivatives. The N2 retrovirus packaged in either of the two murine cell lines, Psi2 and PA317, was used as a model for enveloped viruses. AlPc derivatives were found to be more effective photodynamically for inactivation of the viruses than the corresponding ZnPc derivatives. Sulphonation of the Pc macrocycle reduced its photodynamic activity progressively for both AlPc and ZnPc. Fluoride at 5 mM during light exposure completely protected viruses against inactivation by AlPc. In the presence of F-, inactivation by the sulphonated derivatives AlPcS1 and AlPcS4 was reduced 2.5- and twofold respectively. In a biological membrane (erythrocyte ghosts), F- had no significant effect on AlPcS4-sensitized lipid peroxidation. Under similar conditions, cross-linking of spectrin monomers in ghosts is drastically inhibited (E. Ben-Hur and A. Orenstein, Int. J. Radiat. Biol., 60 (1991) 293-301). Since Pc derivatives do not inactivate non-enveloped viruses, it is hypothesized that inactivation occurs by photodynamic damage to envelope protein(s). Substitution of sulphonic acid residues reduces the binding of Pc derivatives to the envelope protein(s), thereby diminishing their photodynamic efficacy and the ability of F- to modify it.