Contribution of proline‐14 to the structure and actions of melittin

FEBS Letters

Campbell, Iain D.¹  Boheim, Gunther²  Syperek, Inge²  Bazzo, Renzo¹  Harvey, Timothy S.¹  Dempsey, Christopher E.¹ 

[1] Biochemistry Department, Oxford University, South Parks Road, Oxford OX1 3QU, UK;Department of Zellphysiologie, Ruhr Universitat Bochum, Postfach 102148, D-4630 Bochum 1, Germany

关键词: Melittin;    [Ala14]-Melittin;    Nuclear magnetic resonance;    1H;    Hydrogen exchange;    Hemolysis;    Membrane channel;   

DOI  :  10.1016/0014-5793(91)80402-O

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The structure and dynamic properties of bee venom molittin and a synthetic analogue. [Ala¹⁴]-melittin (melittin P14A), are compared, using high resolution ¹H 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.

【 授权许可】

Unknown