Development of metal affinity-immobilized liposome chromatography and its basic characteristics
作者： Hideto Nagami , Hiroshi Umakoshi , Takenori Kitaura , Gary Lee Thompson , Toshinori Shimanouchi
DOI: 10.1016/J.BEJ.2013.12.017
关键词:
摘要: Abstract Metal affinity-immobilized liposome chromatography (MA-ILC) was newly developed as a chromatographic technique to separate and analyze peptides. The MA-ILC matrix gel first prepared by immobilizing liposomes modified with functional ligands. ligand used adsorb metal ions N -hexadecyl iminodiacetic acid (HIDA), which is obtained attaching long alkyl chain an (IDA). Cu(II) ion adsorbed on the through its complex formation HIDA surface of immobilized liposome. Synthetic peptides various types ranging in size from 5 40 residues were then used, their retention properties evaluated. property using usual imidazole elution compared case affinity (IMAC) (ILC). It found that has features both IMAC ILC; ability depends number histidine membrane Histidine tryptophan among amino indicated high contribution coefficient for peptide MA-ILC, probably due interaction properties, respectively.
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