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首页> 外文期刊>Journal of chromatography, A: Including electrophoresis and other separation methods >Selectivity differences in the separation of amphipathic alpha-helical peptides during reversed-phase liquid chromatography at pHs 2.0 and 7.0 - Effects of different packings, mobile phase conditions and temperature
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Selectivity differences in the separation of amphipathic alpha-helical peptides during reversed-phase liquid chromatography at pHs 2.0 and 7.0 - Effects of different packings, mobile phase conditions and temperature

机译：在pH值为2.0和7.0的反相液相色谱过程中，两亲性α-螺旋肽分离的选择性差异-不同填料，流动相条件和温度的影响

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摘要

In an ongoing effort to understand the effect of varying reversed-phase high-performance liquid chromatography (RP-HPLC) parameters on the retention behaviour of peptides, necessary for the rational development of separation/optimization protocols, we believe it is important to delineate the contribution of alpha-helical structure to the selectivity of peptide separations. The present study reports the effects of varying column packing, mobile phase conditions and temperature on RP-HPLC retention behaviour at pHs 2.0 and 7.0 of peptides based on the amphipathic peptide sequence Ac-EAEKAAKEXEKAAKEAEK-amide (with position X in the centre of the hydrophobic face of the alpha-helix), where position X is substituted by L- or D-amino acids. At pH 2.0, an increase in trifluoroacetic acid concentration or the addition of sodium perchlorate to a phosphoric acid-based mobile phase had the similar effect of improving peak shape as well as increasing peptide retention time due to ion-pairing effects with the positively-charged peptides; in contrast, at pH 7.0, the addition of salt had little effect save an improvement in peak shape. Temperature was shown to have a complex influence on peptide selectivity due to varying effects on peptide conformation. In addition, subtle effects on peptide selectivity were also noted based on the column packings employed at pHs 2.0 and 7.0. (C) 2004 Elsevier B.V. All rights reserved.
机译：为了不断了解反相高效​​液相色谱（RP-HPLC）参数的变化对肽保留行为的影响，这是合理开发分离/优化方案所必需的，我们认为描述α-螺旋结构对肽分离选择性的贡献。本研究报告了基于两亲性肽序列Ac-EAEKAAKEXEKAAKEAEK-酰胺（X位置位于疏水中心的位置），不同的柱填充，流动相条件和温度对肽在pHs 2.0和7.0下RP-HPLC保留行为的影响（α-螺旋的正面），其中位置X被L-或D-氨基酸取代。在pH 2.0时，三氟乙酸浓度的增加或向基于磷酸的流动相中添加高氯酸钠，具有类似的改善峰形以及增加肽保留时间的效果，这归因于带有正电荷的离子对效应肽;相反，在pH 7.0下，添加盐几乎没有影响，但峰形没有改善。由于对肽构象的变化影响，温度显示出对肽选择性具有复杂的影响。此外，基于在pH 2.0和7.0下使用的色谱柱填料，对肽的选择性也有微妙的影响。 （C）2004 Elsevier B.V.保留所有权利。

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