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Transferred NOE analyses of conformations of peptides as bound to membrane bilayer of phospholipid; mastoparan‐X
Author(s) -
Wakamatsu Kaori,
Higashijima Tsutomu,
Fujino Masahiko,
Nakajima Terumi,
Miyazawa Tatsuo
Publication year - 1983
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 - 10.1016/0014-5793(83)81062-x
Subject(s) - mastoparan , phospholipid , vesicle , chemistry , peptide , bilayer , membrane , molecule , lipid bilayer , stereochemistry , biophysics , crystallography , biochemistry , organic chemistry , biology , receptor , g protein
The 270‐MHz 1 H‐NMR spectra of mastoparan‐X, a tetradecapeptide toxin from hornet venom, have been observed in the presence of vesicles of perdeuterated dilauroylphosphatidylcholine ([ 2 H 64 ]DLPC). By the analysis of transferred nuclear Overhauser effects (TRNOE), the mastoparan‐X molecule as bound to [ 2 H 64 ]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.