S-Allylmercaptoglutathione: the reaction product of allicin with glutathione possesses SH-modifying and antioxidant properties

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• 作者：Rabinkov ; Aharon ; Miron ; Talia ; Mirelman ; David ; Wilchek ; Meir ; Glozman ; Sabina ; Yavin ; Ephraim ; et. al.
• 关键词：Garlic ; Allicin ; S-Allylmercaptoglutathione ; S-Allylmercaptocysteine ; Enzyme inactivation ; Antioxidant activity ; BAPNA ; N-α ; -benzoyl-DL-arginine p-nitro anilide ; CSSA ; S-allylmercaptocysteine ; DEPT ; distortionless enhancement by polarization transfer
• 刊名：Biochimica et Biophysica Acta (BBA)/Molecular Cell Research
• 出版年：2000
• 出版时间：December 11, 2000
• 年：2000
• 卷：1499
• 期：1-2
• 页码：144-153
• 全文大小：291 K

文摘

The reaction between allicin (diallylthiosulfinate), the active component of garlic and reduced glutathione was investigated. The product of this reaction, mixed disulfide S-allylmercaptoglutathione (GSSA) was separated by high performance liquid chromatography and identified by ¹H and ¹³C nuclear magnetic resonance and mass spectroscopy. The reaction is fast (with an apparent bimolecular reaction rate constant of 3.0 M⁻¹ s⁻¹). It is pH-dependent, which reveals a direct correlation to the actual concentration of mercaptide ion (GS⁻). Both GSSA and S-allylmercaptocysteine (prepared from allicin and cysteine) reacted with SH-containing enzymes, papain and alcohol dehydrogenase from Thermoanaerobium brockii yielding the corresponding S-allylmercapto proteins, and caused inactivation of the enzymes. The activity was restored with dithiothreitol or 2-mercaptoethanol. In addition, GSSA also exhibited high antioxidant properties. It showed significant inhibition of the reaction between OH radicals and the spin trap 5,5′-dimethyl-1-pyroline N-oxide in the Fenton system as well as in the UV photolysis of H₂O₂. In ex vivo experiments done with fetal brain slices under iron-induced oxidative stress, GSSA significantly lowered the production levels of lipid peroxides. The similar activity of GSSA and allicin as SH-modifiers and antioxidants suggests that the thioallyl moiety has a key role in the biological activity of allicin and its derivatives.