INDUCED CONFORMATIONAL STATES OF AMPHIPATHIC PEPTIDES IN AQUEOUS LIPID ENVIRONMENTS
INDUCED CONFORMATIONAL STATES OF AMPHIPATHIC PEPTIDES IN AQUEOUS LIPID ENVIRONMENTS
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DOI：
10.1016/s0006-3495(95)80194-3
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发表时间：
1995-01-01
影响因子：
3.4
通讯作者：
PEREZPAYA, E
中科院分区：
文献类型：
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作者：
BLONDELLE, SE;OSTRESH, JM;PEREZPAYA, E
据报道，在反相高效液相色谱（RP-HPLC）中，两亲模型肽在定义的疏水结构域与非极性固定相结合时产生了特定的构象效应。这种诱导的构象被发现特别明显的肽是两相的cu-螺旋构象。这种诱导的两亲构象导致了比使用基于氨基酸的保留系数预测的更晚的洗脱。在本研究中，RP-HPLC观察到的模型肽的诱导构象行为与它们在水溶液和模拟c -18环境中的二级结构相关。所研究的肽的实验保留时间在脂质存在下与其CD光谱相关，而在三氟乙醇存在下与其CD光谱相关性较差。本文提出了一种新的方法来评估水/脂质界面相互作用对多肽二级结构的诱导作用，该方法包括测量与c -18涂层石英板结合的多肽的CD椭圆率。在这种环境下，结合肽的反相高效液相色谱保留时间与CD椭圆度之间存在良好的相关性。
Specific conformational effects have been reported for amphipathic model peptides upon binding of defined hydrophobic domains to nonpolar stationary phases during reversed-phase high performance liquid chromatography (RP-HPLC). Such induced conformations are found to be especially pronounced for peptides that are amphipathic in an cu-helical conformation. Such induced amphipathic conformations resulted in substantially later elution than predicted using amino acid-based retention coefficients. In the present study, the induced conformational behavior of model peptides observed during RP-HPLC was correlated with their secondary structure as determined by circular dichroism (CD) spectroscopy in both aqueous solution and C-18-mimetic environments. The experimental retention times of the peptides studied were found to correlate with their CD spectra in the presence of lipids, whereas a poor correlation was observed with their CD spectra in the presence of trifluoroethanol. A new approach was developed to evaluate the induction of secondary structure in peptides due to interactions al aqueous/lipid interfaces, which involves the measurement of the CD ellipticities of peptides bound to a set of C-18-coated quartz plates. An excellent correlation was found in this environment between the RP-HPLC retention times and CD ellipticities of the bound peptides.