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

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.