| Co-Investigator(Kenkyū-buntansha) |
TAKAGI Makoto Kyushu University, Faculty of Engineering, Professor, 工学部, 教授 (90037739)
KIKUCHI Jun-ichi Kyushu University, Insitute for Fundamental Research in Organic Chemistry, Assoc, 有機化学基礎研究センター, 助教授 (90153056)
OHNO Teruhisa Kyushu University, Faculty of Engineering, Associate Professor, 工学部, 助教授 (10203887)
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| Research Abstract |
1. The following artificial receptors, which are capable of controlling catalytic activities of artificial enzymes, were designed and synthesized : octopus cyclophanes having the induced-fit function, cage-type cyclophanes being recognizable guest molecules through the lock-and-key mechanism, steroid cyclophanes having intermediate character between these structual types of hosts, hexapus cyclophanes as enterobactin models, and functionalized DNA-intercalators.
2. These artificial receptors perform as efficient intracellular receptors in aqueous solutions, reflecting the individual molecular characteristics. In addition, these receptors act as effective cell-surface receptors, when embedded in bilayr membranes formed with synthetic peptide lipids. Especially, a chiral cage-type cyclophane incorporated in a bilayr membrane exhibits chiral recognition behavior toward hydrophobic amino acids, the substrates for artificial enzymes.
3. The artificial vitaminB_6enzymes, each constituted with a bilayr-forming peptide lipid, hydrophobic vitaminB_6derivative, and metal ions, show catalytic performance as transaminase, tryptophan synthase, and aldolase under mild conditions in aqueous media to mediate stereospecific transformation of amino acids.
4. The artificial vitaminB_<12>enzymes, each formed with a hydrophobic vitaminB_<12>derivative and a bilayr-forming lipid, exhibit catalytic functions as methylmalonyl-CoA mutase, glutamate mutase, and alpha-methyleneglutarate mutase. By combination of the artificial enzyme with a co-catalyst capable of activating the substrates, the isomerization reactions accompanied with the carbon-skeleton rearrangement proceed with turnover of the artificial enzyme.
5. A bilayr-type artificial vitaminB_6enzyme having a transaminase activity and a bilayr-type artificial vitaminB_<12>enzyme having a glutamate mutase activity can be interconnected to perform the respective reactions successively.
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