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Accession number;00A0163498
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| Title;Molecular Synchronization on Lipid Membrane; Control of Enzyme Activity by Artificial Cell-surface Receptor. |
| Author;
SASAKI YOSHIHIRO
(Advanced Inst. Sci. and Technol., Nara)
ISHIMARU TAMIKI
(Advanced Inst. Sci. and Technol., Nara)
FUKUDA KENTARO
(Advanced Inst. Sci. and Technol., Nara)
ARIGA KATSUHIKO
(Advanced Inst. Sci. and Technol., Nara)
KIKUCHI JUN'ICHI
(Advanced Inst. Sci. and Technol., Nara)
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Journal Title;Abstracts. Symposium on Biofunctional Chemistry
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Journal Code:L0836A
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ISSN:
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VOL.14th;NO.;PAGE.80-81(1999)
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| Figure&Table&Reference; |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;Signal transduction systems in cells are regarded as integrated circuits for natural devices. Thus principles extracted for such systems through biomimetic approaches could be applicable to development of various artificial molecular devices. We report here on supramolecular functions of various type of synthetic amphiphiles. We have developed a bile acid derivative having an amino group as an artificial cell-surface receptor, which transmits an external signal to an enzyme in collaboration with transmitter. This signal transduction system accompanies phase reorganization of bile acid and matrix lipid. In order to control the switching of signal transduction we now prepared a novel amiphiphiles with an azobenzene core interposed between two aminoalkyl chains as an artificial transmembrane receptor. Upon addition of 1-hydroxy-2-naphthaldehyde as an external signal ligand, it was effectively recognized at both ends of the receptor by forming the corresponding Schiff-base, and followed by phase reorganization of the receptor in the membrane. We found that the transmembrane receptor is capable of performing as a molecular switch for the enzymatic reaction. When we employed a hydrophobized pyridoxal derivative as an artificial cell-surface receptor, the enzymatic activity of LDH was controlled by tryptamine as an external signal. (author abst.) |
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