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• W2279630473 abstract "Membrane-forming lipids have been prepared. These have a-amino acid residue(s) interposed between a polar head moiety and a hydrophobic double-chain segment, peptide lipids. Cationic, anionic, zwitterionic, and nonionic peptide lipids, except for some nonionic ones, undergo aggregation to form multiwalled bilayer vesicles and/or lamellae when these are dispersed in aqueous media. The number of carbon atoms in each hydrocarbon chain of the double-chain portion needs to be equal to or greater than 12. The multiwalled vesicles are transformed into single-walled bilayervesicles upon sonication and the latter are morphologically stable over a sufficiently prolonged period of time. The phase transition parameters, T m and ΔH, of the multiwalled bilayer aggregates are linearly correlated with the alkyl-chain length of the double-chain segment for a series of N+ C5Ala2Cn: ca. 20°C and ca. 10 kJmol-1 changes per two methylene groups, respectively. On the other hand, nonlamellar aggregates, inverted cubic and inverted hexagonal, are formed by proper adjustment of the critical packing parameter for the peptide lipids. Single-walled bilayer vesicles undergo fusion via the formation of the intermediate nonlamellar phase. A bilayer-type artificial enzyme, which can simulate the catalytic functions of vitamin B6-dependent enzymes, is constituted with a hydrophobic vitamin B6, single-walled vesicles of a peptide lipid having a histidyl residue, and copper(II) ions. The artificial enzyme catalyzes transamination between a relatively hydrophobic α-amino acid and a hydrophilic α-keto acid along with the turnover of the catalyst system under mild conditions. The reaction mechanism and the microenvironmental properties of the catalytic site have been clarified. The identical artificial enzyme also simulates the catalytic function of tryptophan synthase that converts serine into tryptophan by β-replacement of the former amino acid with indole." @default.
• W2279630473 created "2016-06-24" @default.
• W2279630473 creator A5014644883 @default.
• W2279630473 creator A5034283472 @default.
• W2279630473 date "1991-01-01" @default.
• W2279630473 modified "2023-09-26" @default.
• W2279630473 title "Supramolecular Assemblies Formed with Synthetic Peptide Lipids. Functional Models of Biomembranes and Enzymes" @default.
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• W2279630473 doi "https://doi.org/10.1007/978-3-642-76241-3_3" @default.
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