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Synthesis of symmetric disulfides as potential alternative substrates for trypanothione reductase and glutathione reductase: Part 1



Synthesis of symmetric disulfides as potential alternative substrates for trypanothione reductase and glutathione reductase: Part 1



Amino Acids 9(4): 327-342



The synthesis of a series of symmetrical disulfides as potential substrates of trypanothione reductase and glutathione reductase was described. The key intermediate in the synthetic approach was the choice of S-(t)butylmercapto-L-cysteine (1). The spermidine ring in the native substrate, trypanothione disulfide (TSST), was replaced with 3-dimethyl-aminopropylamine (DMAPA), while theγ-Glu moiety was replaced by phenylalanyl or tryptophanyl residues. The same modifications in theγ-Glu moiety of glutathione disulfide (GSSG) were applied.

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Accession: 009510044

Download citation: RISBibTeXText

PMID: 24178881

DOI: 10.1007/BF00807270


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