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Solution conformation of an ET B selective agonist, ET‐1[Cys(Acm) 1,15 ,Ala 3 ,Leu 7 ,Aib 11 ], in CD 3 OH/H 2 O by 1 H NMR and molecular modelling
Author(s) -
Hewage Chandralal M,
Jiang Lu,
Parkinson John A,
Ramage Robert,
Sadler Ian H
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00239-7
Subject(s) - chemistry , agonist , endothelin receptor , stereochemistry , nuclear magnetic resonance spectroscopy , solvent , peptide , endothelin 3 , receptor , endothelins , biochemistry
To understand the basic structural requirements for the biological activity of endothelin peptides, the solution structure of an ET B selective agonist, ET‐1[Cys(Acm) 1,15 ,Ala 3 ,Leu 7 ,Aib 11 ], was investigated by 1 H NMR spectroscopy and molecular modelling. The structure is characterised by an α‐helical conformation between residues Ser 5 ‐His 16 but is undefined at both the N and C termini. To date, neither the solution structures of linear modified peptides nor the effects of a methanol/water solvent system have been examined for endothelin or endothelin‐like peptides. This structure plays an important role towards the design of endothelin receptor selective agonists and antagonists.