Motilin–bicelle interactions: membrane position and translational diffusion

FEBS Letters

Andersson, August¹  Mäler, Lena¹ 

[1] Department of Biochemistry and Biophysics, Arrhenius Laboratory, Stockholm University, 10691 Stockholm, Sweden

关键词: Motilin;    Bicelle;    Nuclear magnetic resonance;    Pulsed field gradient;    Diffusion;    DHPC;    1;    2-dihexanoyl-sn-glycero-3-phosphatidylcholine;    DMPC;    1;    2-dimyristoyl-sn-glycero-3-phosphatidylcholine;    DMPG;    1;    2-dimyristoyl-sn-glycero-3-phospho-1-glycerol;    PFG;    pulsed field gradient;    SDS;    sodium dodecyl sulfate;    TOCSY;    total correlation spectroscopy;    cmc;    critical micelle concentration;    TMS;    tetramethylsilane;   

DOI  :  10.1016/S0014-5793(03)00514-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The interaction between the peptide hormone motilin and bicelles has been investigated by pulsed field gradient-nuclear magnetic resonance methods and by the use of paramagnetic probes. Diffusion coefficients were measured for motilin, the phospholipids with and without motilin, and for tetramethylsilane. The results show that around 90% of motilin is bound to acidic bicelles and 84% of motilin is bound to neutral bicelles. It is found that the apparent bicelle size is reduced by the presence of motilin. This cannot be explained by changes in 1,2-dihexanoyl-sn-glycero-3-phosphatidylcholine solubility. The use of paramagnetic agents to investigate the position of motilin shows that the turn in the N-terminus of motilin is inserted into the bicelle, while the helix most likely resides within the head-group layer.

【 授权许可】

Unknown