TY - JOUR
T1 - Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 2
T2 - Substitution of the glycine part
AU - Amssoms, Katie
AU - Oza, Sandra L.
AU - Augustyns, Koen
AU - Yamani, Abdellah
AU - Lambeir, Anne-Marie
AU - Bal, Gunther
AU - Van der Veken, Pieter
AU - Fairlamb, Alan H.
AU - Haemers, Achiel
PY - 2002/10/7
Y1 - 2002/10/7
N2 - Glutathionylspermidine synthetase (GspS) is an essential enzyme in the biosynthesis of trypanothione and is an attractive target for the design of selective anti-parasitic drugs. We synthesised a series of analogues of glutathione (L-γ-Glu-L-Leu-X) where the glycine moiety has been substituted for other amino acids. These peptides were evaluated as substrates and inhibitors of GspS. Compounds with basic side chains such as diaminopropionic acid were found to be good inhibitors (Ki: 7.2 μM). Substitution of the glycine part abolished the GspS substrate properties of the tripeptide.
AB - Glutathionylspermidine synthetase (GspS) is an essential enzyme in the biosynthesis of trypanothione and is an attractive target for the design of selective anti-parasitic drugs. We synthesised a series of analogues of glutathione (L-γ-Glu-L-Leu-X) where the glycine moiety has been substituted for other amino acids. These peptides were evaluated as substrates and inhibitors of GspS. Compounds with basic side chains such as diaminopropionic acid were found to be good inhibitors (Ki: 7.2 μM). Substitution of the glycine part abolished the GspS substrate properties of the tripeptide.
UR - http://www.scopus.com/inward/record.url?scp=0037037377&partnerID=8YFLogxK
U2 - 10.1016/S0960-894X(02)00538-3
DO - 10.1016/S0960-894X(02)00538-3
M3 - Article
C2 - 12217358
AN - SCOPUS:0037037377
SN - 0960-894X
VL - 12
SP - 2703
EP - 2705
JO - Bioorganic and Medicinal Chemistry Letters
JF - Bioorganic and Medicinal Chemistry Letters
IS - 19
ER -