Development of metal affinity-immobilized liposome chromatography and its basic characteristics

Hideto Nagami, Hiroshi Umakoshi, Takenori Kitaura, Gary Lee Thompson, Toshinori Shimanouchi, Ryoichi Kuboi

Research output: Contribution to journalArticle

4 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)66-73
Number of pages8
JournalBiochemical Engineering Journal
Volume84
DOIs
Publication statusPublished - Mar 15 2014
Externally publishedYes

Fingerprint

Liposomes
Chromatography
Metals
Peptides
Affinity chromatography
Ions
Affinity Chromatography
Histidine
Metal ions
Acids
Gels
Ligands
Membranes
Tryptophan
Gel Chromatography
Amino acids
Amino Acids

Keywords

  • Chromatography
  • Immobilization
  • Liposome
  • Metal affinity

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biomedical Engineering
  • Environmental Engineering

Cite this

Development of metal affinity-immobilized liposome chromatography and its basic characteristics. / Nagami, Hideto; Umakoshi, Hiroshi; Kitaura, Takenori; Thompson, Gary Lee; Shimanouchi, Toshinori; Kuboi, Ryoichi.

In: Biochemical Engineering Journal, Vol. 84, 15.03.2014, p. 66-73.

Research output: Contribution to journalArticle

Nagami, Hideto ; Umakoshi, Hiroshi ; Kitaura, Takenori ; Thompson, Gary Lee ; Shimanouchi, Toshinori ; Kuboi, Ryoichi. / Development of metal affinity-immobilized liposome chromatography and its basic characteristics. In: Biochemical Engineering Journal. 2014 ; Vol. 84. pp. 66-73.
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