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首页> 外文期刊>Applied Magnetic Resonance >Membrane-peptide interaction studied by PELDOR and CW ESR: Peptide conformations and cholesterol effect on the spatial peptide distribution in the membrane
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Membrane-peptide interaction studied by PELDOR and CW ESR: Peptide conformations and cholesterol effect on the spatial peptide distribution in the membrane

机译：通过PELDOR和CW ESR研究膜-肽相互作用：肽构象和胆固醇对膜中空间肽分布的影响

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摘要

Pulsed electron-electron double resonance (PELDOR) combined with continuous-wave electron paramagnetic resonance was used to study inter- and intramolecular dipole-dipole interactions between spin labels for spin-labeled analogs of trichogin GA IV bound to multilamellar membranes of egg L-a-phosphatidylcholine (ePC) and in ePC membranes containing cholesterol. All samples were frozen to 77 K. For mono-labeled peptide concentrations in lipid over the range between 0.5 to 2.2 mol%, it is shown that in these membranes trichogin molecules are distributed homogeneously and are likely to be located on or near the inner and outer membrane surfaces. Addition of cholesterol to a final concentration of 16.5 mol% leads to an increase of the local concentration of trichogin molecules in the membranes. For the double-labeled trichogin, a distribution of the intramolecular distance between the two spin labels was observed. The distribution function is characterized by two main maxima located at distances of 1.3 and 1.8 nm. The distance of 1.3 nm is close to that expected for the alpha-helix structure of the peptide chain. The distance of 1.8 nun corresponds to a mixed structure in which a 3(10) helix is combined with a set of even more elongated conformations.
机译：脉冲电子双共振（PELDOR）与连续波电子顺磁共振结合用于研究自旋标记的Trichogin GA IV自旋标记类似物与鸡蛋La-磷脂酰胆碱的多层膜结合的自旋标记之间的分子间和分子内偶极-偶极相互作用。 （ePC）和含有胆固醇的ePC膜中。将所有样品冷冻至77K。对于脂质中单标记肽浓度在0.5到2.2 mol％之间的范围，表明滴虫蛋白分子均匀分布并且很可能位于内部和周围。外膜表面。将胆固醇添加至16.5mol％的最终浓度导致膜中滴虫蛋白分子的局部浓度增加。对于双标记的滴虫蛋白，观察到两个自旋标记之间的分子内距离的分布。分布函数的特征是位于1.3和1.8 nm处的两个主要最大值。 1.3 nm的距离接近于肽链的α-螺旋结构所预期的距离。 1.8 nun的距离对应于一个混合结构，其中3（10）螺旋与一组甚至更长的构象结合在一起。

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