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

R Jaouhari; T Besheya; J H McKie; K T Douglas

doi:10.1007/BF00807270

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

Amino Acids. 1995 Dec;9(4):327-42. doi: 10.1007/BF00807270.

Authors

R Jaouhari¹, T Besheya, J H McKie, K T Douglas

Affiliation

¹ Pharmacy Department, University of Manchester, Manchester, United Kingdom.

PMID: 24178881
DOI: 10.1007/BF00807270

Abstract

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.