Biological activities of [Thr2]sarafotoxin-b, a synthetic analogue of sarafotoxin-b

H. Lamthanh, A. Bdolah*, C. Creminon, J. Grassi, A. Menez, Z. Wollberg, E. Kochva

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


The 21 amino acid sarafotoxins (SRTX) c and d/e as well as endothelin-3 (ET-3) are known to be less toxic and weaker pharmacologically than the other isopeptides SRTX-a, SRTX-b and ET-1. Since SRTX-c, SRTX-d/e and ET-3 possess a Thr instead of a Ser at position 2, we investigated the possibility that this mutation could be responsible for the observed biological differences. Here we show that the synthetic [Thr2]SRTX-b has indeed a lower vasoconstriction efficacy (≈35%) in the rabbit aorta, but it is nearly as potent as SRTX-b in toxicity tests and in influencing contraction of the rat uterus. Using monoclonal antibodies directed against the structurally related endothelin-1, we also show that the antigenicity of the analogue is comparable to that of SRTX-b, suggesting that the overall structure of the two peptides is similar, despite the substitution at position 2. We suggest that the Thr2 substitution contributes to the lower activity of the 'weak' peptides in some systems; however, additional substitutions found in the 'weak' peptides of the ET/SRTX family most probably contribute to their low pharmacological activity.

Original languageEnglish
Pages (from-to)1105-1114
Number of pages10
Issue number9
StatePublished - Sep 1994


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