Development of metal affinity-immobilized liposome chromatography and its basic characteristics |
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| Affiliation: | 1. Divisions of Gastroenterology and Hepatology, Keck School of Medicine of USC, Los Angeles, CA;2. Divisions of Gastroenterology and Hepatology, Washington University School of Medicine, St. Louis, Mo;3. Department of Medicine, St. Louis Health Care System, St. Louis, Mo;1. Department of Paediatrics, University of Calgary Faculty of Medicine and Alberta Children’s Hospital Research Institute, Calgary, Alberta, Canada;2. Department of Pathology (Neuropathology), University of Calgary Faculty of Medicine and Alberta Children’s Hospital Research Institute, Calgary, Alberta, Canada;3. Department of Pathology (Paediatric), University of Calgary Faculty of Medicine and Alberta Children’s Hospital Research Institute, Calgary, Alberta, Canada;4. Department of Clinical Neurosciences, University of Calgary Faculty of Medicine and Alberta Children’s Hospital Research Institute, Calgary, Alberta, Canada;1. Institute of Pharmacology and Toxicology, University of Ulm Medical Center, Ulm, Germany;2. Rudolf-Virchow-Center, DFG-Research Center for Experimental Biomedicine, University of Würzburg, Würzburg, Germany;3. Institute of Organic Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary;4. School of Engineering and Science, Jacobs University Bremen, Bremen, Germany;1. Department of Pharmacy and Guangdong Province Key Laboratory of Pharmacodynamic Constituents of Traditional Chinese Medicine & New Drug Research, Jinan University, Guangzhou 510632, China;2. Laboratory of Analytical Pharmaceutical Chemistry, Department of Pharmaceutical Sciences, University of Liege, CHU B36, Liege B-4000, Belgium |
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| 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 was first prepared by immobilizing liposomes modified with functional ligands. The functional ligand used to adsorb metal ions was N-hexadecyl iminodiacetic acid (HIDA), which is obtained by attaching a long alkyl chain to an iminodiacetic acid (IDA). Cu(II) ion was first adsorbed on the gel matrix through its complex formation with the HIDA on the surface of the immobilized liposome. Synthetic peptides of various types ranging in size from 5 to 40 residues were then used, and their retention properties on the MA-ILC were evaluated. The retention property of peptides on the MA-ILC by using a usual imidazole elution was compared with the retention property in the case of the immobilized metal affinity chromatography (IMAC) and an immobilized liposome chromatography (ILC). It was found that the retention property of peptides on the MA-ILC has the features of both the IMAC and the ILC; the retention ability of peptides depends on both the number of histidine residues in peptides and the liposome membrane affinity of the peptides. Histidine and tryptophan residues among amino acid residues in peptides indicated a high contribution coefficient for the peptide retention on the MA-ILC, probably due to their metal ion and membrane interaction properties, respectively. |
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| Keywords: | Metal affinity Liposome Immobilization Chromatography |
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