FEBS Letters | |
Contribution of proline‐14 to the structure and actions of melittin | |
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
【 预 览 】
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