The interaction of amino-deuteromethylated melittin with phospholipid membranes studied by deuterium NMR.

Abstract:

:Melittin, deuteromethylated on each of the four amino groups (Gly-1 N alpha and Lys-7, 21, and 23 N epsilon), was prepared by reductive methylation using deuteroformaldehyde and NaBD3CN. Deuterium NMR spectra were obtained for the modified peptide (D-melittin) bound to phospholipid bilayers and erythrocyte ghosts. D-Melittin at 4 mol% (peptide:lipid) induced reversible transitions between extended bilayers and micelles at the phase-transition temperature in dimyristoylphosphatidylcholine (DMPC) bilayers. These changes in lipid morphology did not occur at 1 mol% D-melittin: DMPC and the peptide was highly motionally restricted in gel in gel-phase lipid.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Dempsey CE,Cryer GD,Watts A

doi

10.1016/0014-5793(87)81041-4

subject

Has Abstract

pub_date

1987-06-22 00:00:00

pages

173-7

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(87)81041-4

journal_volume

218

pub_type

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