Transferred NOE analyses of conformations of peptides as bound to membrane bilayer of phospholipid; mastoparan‐X

FEBS Letters

Nakajima, Terumi¹  Miyazawa, Tatsuo³  Higashijima, Tsutomu³  Wakamatsu, Kaori³  Fujino, Masahiko² 

[1] Institute for Medical and Dental Engineering, Tokyo Medical and Dental University, Chiyoda-ku, Tokyo 101, Japan;Chemical Laboratories, Central Research Division, Takeda Chemical Industries, Yodogawa-ku, Osaka 532, Japan;Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Bunkyo-ku, Tokyo 113, Japan

关键词: 1H-NMR;    Mastoparan-X;    Membrane-bound conformation;    Perdeuterated phosphatidylcholine;    Physiologically active peptide;    Transferred NOE;   

DOI  :  10.1016/0014-5793(83)81062-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The 270-MHz ¹H-NMR spectra of mastoparan-X, a tetradecapeptide toxin from hornet venom, have been observed in the presence of vesicles of perdeuterated dilauroylphosphatidylcholine ([²H₆₄]DLPC). By the analysis of transferred nuclear Overhauser effects (TRNOE), the mastoparan-X molecule as bound to [²H₆₄]DLPC vesicles is found to take an α-helical form in the C-terminal (and central) part. The TRNOE analysis with perdeuterated phospholipid is a unique method for the elucidation of conformation of peptide (and drug) molecules as bound to phospholipid membranes.

【 授权许可】

Unknown