Design of C-terminal peptide antagonists of endothelin: structure-activity relationships of ET-[16–21, D-His 16]

We have previously described structure-activity relationships in the hydrophobic C-terminal hexapeptide region of ET-1 known to be highly important for receptor recognition. A mono- D -amino acid scan of ET[16–21] revealed that a D-His 16 substitution gave rise to endothelin antagonists. We will des...

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Bibliographic Details
Published in:Bioorganic & medicinal chemistry letters 1993-04, Vol.3 (4), p.497-502
Main Authors: Doherty, A.M., Cody, W.L., He, J.X., DePue, P.L., Leonard, D.M., Dunbar, J.B., Hill, K.E., Flynn, M.A., Reynolds, E.E.
Format: Article
Language:English
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Summary:We have previously described structure-activity relationships in the hydrophobic C-terminal hexapeptide region of ET-1 known to be highly important for receptor recognition. A mono- D -amino acid scan of ET[16–21] revealed that a D-His 16 substitution gave rise to endothelin antagonists. We will describe the discovery and development of further antagonists in this series. Structure-activity relationships of endothelin antagonists derived from the C-terminus of ET-1 are described.
ISSN:0960-894X
1464-3405
DOI:10.1016/S0960-894X(01)81215-4