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Contribution of proline‐14 to the structure and actions of melittin
Author(s) -
Dempsey Christopher E.,
Bazzo Renzo,
Harvey Timothy S.,
Syperek Inge,
Boheim Gunther,
Campbell Iain D.
Publication year - 1991
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(91)80402-o
Subject(s) - melittin , chemistry , biophysics , helix (gastropod) , alpha helix , stereochemistry , peptide , circular dichroism , biochemistry , biology , ecology , snail
The structure and dynamic properties of bee venom molittin and a synthetic analogue. [Ala 14 ]‐melittin (melittin P14A), are compared, using high resolution 1 H nuclear magnetic resonance (NMR) spectroscopy and amide exchange measurements in methanol. P14A is shown to adopt a regular, stable α‐helical conformation in solution without the flexibility around the Pro‐14 residue found in melittin. P14A has twice the hemolytic activity of melittin but is less able to induce voltage‐dependent ion conductance in planar bilayers. The results indicate that helix flexibility afforded by the Pro‐14 residue promotes the ability of melittin to adopt the transbilayer associates thought to underlie ion translocation.