Hydrolase-like activity provided by zinc(Ii) and oleoyl-histidine at liposome membrane surface

Atsushi Tauchi, Keishi Suga, Hiroshi Umakoshi

Research output: Contribution to journalArticlepeer-review

Abstract

Carbonic anhydrase (CA) is a hydrolase enzyme possessing an active center composed of three histidines (His), zinc(II) (Zn2+ ), and a hydration water. Here we report the hydrolase-like catalytic activity provided by the oleoyl-histidine (O-His) modified on liposome membranes. O-His was synthesized by the amide bond between oleic acid and His, and was incorporated into 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) liposomes. The hydrolysis of p-nitrophenylacetate was promoted by O-His modified DOPC liposomes in the presence of Zn2+ . The formation of the active center was revealed by UV resonance Raman spectra. We conclude that the liposome membrane surface can be utilized as a platform for artificial hydrolysis reactions by modifying essential ligands inspired from natural enzymes.

Original languageEnglish
Article number24
JournalColloids and Interfaces
Volume2
Issue number2
DOIs
Publication statusPublished - 2018
Externally publishedYes

Keywords

  • Artificial enzyme
  • Histidine
  • Liposome
  • Membrane interface
  • Zinc(II)

ASJC Scopus subject areas

  • Chemistry (miscellaneous)
  • Colloid and Surface Chemistry

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