TY - JOUR
T1 - Hydrolase-like activity provided by zinc(Ii) and oleoyl-histidine at liposome membrane surface
AU - Tauchi, Atsushi
AU - Suga, Keishi
AU - Umakoshi, Hiroshi
N1 - Funding Information:
Acknowledgments: This research was supported by the Japan Society for the Promotion of Science (JSPS) Grant-in-Aid for Scientific Research A (26249116), JSPS Grant-in-Aid for Young Scientist B (16K18279), and JSPS Grant-in-Aid for Challenging Exploratory Research (T15K142040).
Publisher Copyright:
© 2018 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2018
Y1 - 2018
N2 - 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.
AB - 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.
KW - Artificial enzyme
KW - Histidine
KW - Liposome
KW - Membrane interface
KW - Zinc(II)
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U2 - 10.3390/colloids2020024
DO - 10.3390/colloids2020024
M3 - Article
AN - SCOPUS:85104492562
SN - 2504-5377
VL - 2
JO - Colloids and Interfaces
JF - Colloids and Interfaces
IS - 2
M1 - 24
ER -