4.0 Article Proceedings Paper

Control of enzymic activity by artificial cell-surface receptors

Journal

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 11, Issue 4-6, Pages 977-984

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/S1381-1177(00)00019-9

Keywords

lactate dehydrogenase; protein-lipid interaction; artificial receptor; bile acid; signal transduction

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A novel type of artificial cell-surface receptor capable of affecting enzymic activity was designed by employing steroidal moiety. Bile acid derivatives having an amino group, effectively recognized both the aromatic aldehydes and copper(II) ions in bilayer membrane formed with a synthetic peptide lipid. On the other hand, pig heart L-lactate dehydrogenase (LDH) was bound to the bilayer membrane surface mainly through electrostatic interactions, and the LDH activity was specifically inhibited by copper(LI) ions. On these grounds, we constituted artificial signaling systems in combinations, with a steroidal receptor, a bilayer-forming synthetic lipid, and LDH. The present supramolecular vesicles acted as nano-reactors in which the artificial receptor was able to switch on the enzymic activity via accompanying double signal recognition and phase reorganization (C) 2001 Elsevier Science B.V. All rights reserved.

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