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Colloids Interfaces 2018, 2(2), 24; https://doi.org/10.3390/colloids2020024

Hydrolase-Like Activity Provided by Zinc(II) and Oleoyl-Histidine at Liposome Membrane Surface

Division of Chemical Engineering, Graduate School of Engineering Science, Osaka University, 1–3 Machikaneyama-cho, Toyonaka, Osaka 560-8531, Japan
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Received: 20 April 2018 / Revised: 8 June 2018 / Accepted: 11 June 2018 / Published: 13 June 2018
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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. View Full-Text
Keywords: artificial enzyme; liposome; membrane interface; histidine; Zinc(II) artificial enzyme; liposome; membrane interface; histidine; Zinc(II)
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Tauchi, A.; Suga, K.; Umakoshi, H. Hydrolase-Like Activity Provided by Zinc(II) and Oleoyl-Histidine at Liposome Membrane Surface. Colloids Interfaces 2018, 2, 24.

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