Conformational study of three endothelin antagonists with 1H NMR at low temperature and molecular dynamics

FEBS Letters

Paye, Ingrid²  Demaude, Thierry²  Scarso, Alain²  Van Binst, Georges¹  Verheyden, Patricia¹  Brichard, Marie-Hélène²  Van Assche, Ivo² 

[1] Department of Organic Chemistry, Vrije Universiteit Brussel, Pleinlaan, B-1050 Brussel, Belgium;UCB Bioproducts, Chemin du Foriest, B-1420 Braine-L'Alleud, Belgium

关键词: Endothelin;    Antagonist;    BQ123;    1H NMR;    MD;   

DOI  :  10.1016/0014-5793(94)00352-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The conformations of three endothelin antagonists, a cyclic pentapeptide, a linear tripeptide and a linear hexapeptide, are compared by ¹H NMR and molecular dynamics. The three analogues have a Leu and a dTrp side chain which are oriented parallel, and an acidic group next to the dTrp residue.

【 授权许可】

Unknown