Conformational behavior of the linear hexapeptide senktide: A receptor specific tachykinin analog

FEBS Letters

Ferretti, James A.¹  Sumner, Susan C.J.¹ 

[1] Laboratory of Chemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA

关键词: Receptor selective;    Conformational restriction;    NMR;    2D;    CD;   

DOI  :  10.1016/0014-5793(89)80942-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A receptor selective linear hexapeptide tachykinin analog, senktide, is shown to be highly ordered in solution. The conformational restriction is attributed to steric and electrostatic interactions produced by N-methylation of the third amino acid residue in the sequence and the negatively charged N-terminus. The structure of senktide is described as a dynamic mixture of similar conformations where the predominant one is a distorted antiparallel hydrogen bonded β-pleated sheet. The observed senktide-receptor specificity is suggested to result from a selection of this or a closely related conformation.

【 授权许可】

Unknown