期刊论文详细信息
FEBS Letters
Phospholipid phase transitions in homogeneous nanometer scale bilayer discs
Shaw, Andrew W2  Sligar, Stephen G2  McLean, Mark A1 
[1]Department of Biochemistry, University of Illinois, Urbana, IL 61801, USA
[2]Department of Chemistry, University of Illinois, Urbana, IL 61801, USA
关键词: Phospholipid;    Phase transition;    Laurdan;    Generalized polarization;    Differential scanning calorimetry;    MSP;    membrane scaffold protein;    DPPC;    dipalmitoyl phosphatidylcholine;    DMPC;    dimyristoyl phosphatidylcholine;    Laurdan;    6-dodecanoyl-2-dimethylaminonaphthalene;    DPH;    1;    6-diphenyl-1;    3;    5-hexatriene;    GP;    generalized polarization;    DSC;    differential scanning calorimetry;   
DOI  :  10.1016/S0014-5793(03)01400-5
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

Nanoscale protein supported phospholipid bilayer discs, or Nanodiscs, were produced for the purpose of studying the phase transition behavior of the incorporated lipids. Nanodiscs and vesicles were prepared with two phospholipids, dipalmitoyl phosphatidylcholine and dimyristoyl phosphatidylcholine, and the phase transition of each was analyzed using laurdan fluorescence and differential scanning calorimetry. Laurdan is a fluorescent probe sensitive to the increase of hydration in the lipid bilayer that accompanies the gel to liquid crystalline phase transition. The emission intensity profile can be used to derive the generalized polarization, a measure of the relative amount of each phase present. Differential scanning calorimetry was used to further quantitate the phase transition of the phospholipids. Both methods revealed broader transitions for the lipids in Nanodiscs compared to those in vesicles. Also, the transition midpoint was shifted 3–4°C higher for both lipids when incorporated into Nanodiscs. These findings are explained by a loss of cooperativity in the lipids of Nanodiscs which is attributable to the small size of the Nanodiscs as well as the interaction of boundary lipids with the protein encircling the discs. The broad transition of the Nanodisc lipid bilayer better mimics the phase behavior of cellular membranes than vesicles, making Nanodiscs a ‘native-like’ lipid environment in which to study membrane associated proteins.

【 授权许可】

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