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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Influence of N-dodecyl-N,N-dimethylamine N-oxide on the activity of sarcoplasmic reticulum Ca(2+)-transporting ATPase reconstituted into diacylphosphatidylcholine vesicles: efects of bilayer physical parameters.
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Influence of N-dodecyl-N,N-dimethylamine N-oxide on the activity of sarcoplasmic reticulum Ca(2+)-transporting ATPase reconstituted into diacylphosphatidylcholine vesicles: efects of bilayer physical parameters.

机译：N-十二烷基-N，N-二甲胺N-氧化物对肌质网Ca（2 +）-运输ATPase的活性重构为二酰基磷脂酰胆碱囊泡的影响：双层物理参数的影响。

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摘要

Sarcoplasmic reticulum Ca-transporting ATPase (EC 3.6.1.38) was isolated from rabbit white muscle, purified and reconstituted into vesicles of synthetic diacylphosphatidylcholines with monounsaturated acyl chains using the cholate dilution method. In fluid bilayers at 37 degrees C, the specific activity of ATPase displays a maximum (31.5+/-0.8 IU/mg) for dioleoylphosphatidylcholine (diC18:1PC) and decreases progressively for both shorter and longer acyl chain lengths. Besides the hydrophobic mismatch between protein and lipid bilayer, changes in the bilayer hydration and lateral interactions detected by small angle neutron scattering (SANS) can contribute to this acyl chain length dependence. When reconstituted into dierucoylphosphatidylcholine (diC22:1PC), the zwitterionic surfactant N-dodecyl-N,N-dimethylamine N-oxide (C12NO) stimulates the ATPase activity from 14.2+/-0.6 to 32.5+/-0.8 IU/mg in the range of molar ratios C12NO:diC22:1PC=0/1.2. In dilauroylphosphatidylcholines (diC12:0PC) and diC18:1PC, the effect of C12NO is twofold-the ATPase activity is stimulated at low and inhibited at high C12NO concentrations. In diC18:1PC, it is observed an increase of activity induced by C12NO in the range of molar ratios C12NO:diC18:1PC< or =1.3 in bilayers, where the bilayer thickness estimated by SANS decreases by 0.4+/-0.1 nm. In this range, the 31P-NMR chemical shift anisotropy increases indicating an effect of C12NO on the orientation of the phosphatidylcholine dipole N(+)-P- accompanied by a variation of the local membrane dipole potential. A decrease of the ATPase activity is observed in the range of molar ratios C12NO:diC18:1PC=1.3/2.5, where mixed tubular micelles are detected by SANS in C12NO+diC18:1PC mixtures. It is concluded that besides hydrophobic thickness changes, the changes in dipole potential and curvature frustration of the bilayer could contribute as well to C12NO effects on Ca(2+)-ATPase activity.
机译：从胆白中分离出肌质网钙转运ATP酶（EC 3.6.1.38），纯化后，用胆酸盐稀释法将其重构为具有单不饱和酰基链的合成二酰基磷脂酰胆碱的囊泡。在37°C的流体双层中，ATPase的比活对油酰磷脂酰胆碱（diC18：1PC）表现出最大值（31.5 +/- 0.8 IU / mg），对于较短和较长的酰基链长度都逐渐降低。除了蛋白质和脂质双层之间的疏水失配以外，双层水合和小角度中子散射（SANS）检测到的横向相互作用的变化也可导致这种酰基链长度依赖性。两性离子表面活性剂N-十二烷基-N，N-二甲基胺N-氧化物（C12NO）重构为二十二烷基磷脂酰胆碱（diC22：1PC）时，其ATPase活性从14.2 +/- 0.6增至32.5 +/- 0.8 IU / mg C12NO：diC22：1PC = 0 / 1.2的摩尔比。在二月桂酰磷脂酰胆碱（diC12：0PC）和diC18：1PC中，C12NO的作用是双重的-在低C12NO浓度下刺激ATPase活性，而在高C12NO浓度下抑制。在diC18：1PC中，观察到在双层中摩尔比C12NO：diC18：1PC <或= 1.3的范围内，由C12NO诱导的活性增加，其中SANS估计的双层厚度降低了0.4 +/- 0.1 nm。在此范围内，31P-NMR化学位移各向异性增加，表明C12NO对磷脂酰胆碱偶极N（+）-P-的取向产生影响，并伴随着局部膜偶极电位的变化。在摩尔比C12NO：diC18：1PC = 1.3 / 2.5的范围内观察到ATPase活性的降低，其中SANS在C12NO + diC18：1PC混合物中检测到混合的管状胶束。结论是，除了疏水性厚度变化之外，双层的偶极电势和曲率抑制的变化也可能对C12NO对Ca（2 +）-ATPase活性的影响有贡献。

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