Fürtös-Matei A, Day R, St-Pierre S A, St-Pierre L G, Waldron K C
Département de Chimie, Université de Montréal, Québec, Canada.
Electrophoresis. 2000 Mar;21(4):715-23. doi: 10.1002/(SICI)1522-2683(20000301)21:4<715::AID-ELPS715>3.0.CO;2-5.
Prodynorphin is a precursor that has multiple cleavage sites to release various dynorphin opioid peptides. The dynorphin analogs used in this study have 18 amino acid residues. A series of dynorphin-like peptides, differing by a single residue (alanine substitution) were assembled by Fmoc solid-phase procedures and purified by preparative high performance liquid chromatography (HPLC). Separation of the Ala-scan dynorphin analogs was investigated by micellar electrokinetic chromatography (MEKC) employing anionic, cationic and zwitterionic surfactants. The role of electrostatic and hydrophobic forces in analyte-surfactant interactions is discussed with respect to the observed elution patterns. Separation of all dynorphin analogs by MEKC using a zwitterionic surfactant shows this technique to be powerful for separating closely related peptide species. It also demonstrates the potential for using MEKC for the prescreening of peptide libraries to determine their biological activity toward specific receptors. Results from the separation of dynorphin analogs by free solution and ion-pairing capillary electrophoresis are also presented.
前强啡肽是一种前体，具有多个切割位点以释放各种强啡肽阿片肽。本研究中使用的强啡肽类似物有18个氨基酸残基。通过Fmoc固相程序组装了一系列相差一个残基（丙氨酸取代）的类强啡肽肽，并通过制备型高效液相色谱（HPLC）进行纯化。采用阴离子、阳离子和两性离子表面活性剂，通过胶束电动色谱（MEKC）研究丙氨酸扫描强啡肽类似物的分离。根据观察到的洗脱模式，讨论了静电和疏水力在分析物 - 表面活性剂相互作用中的作用。使用两性离子表面活性剂通过MEKC分离所有强啡肽类似物表明，该技术对于分离密切相关的肽类物质非常有效。它还证明了使用MEKC对肽库进行预筛选以确定其对特定受体的生物活性的潜力。还展示了通过自由溶液和离子对毛细管电泳分离强啡肽类似物的结果。
