| Co-Investigator(Kenkyū-buntansha) |
YOSHIMIZU Hiroaki Nagoya Institute of Technology, Faculty of Engineering, Assistant Professor, 工学部, 助手 (10240350)
TSUJITA Yoshiharu Nagoya Institute of Technology, Faculty of Engineering, Professor, 工学部, 教授 (70016591)
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| Research Abstract |
Amphiphilic polypeptides, poly( gamma-methyl L-glutamate)-block-poly(ethylene glycol), PMLG-PEG, and poly(gamma -benzyl L-glutamate)-block-poly(ethylene glycol), PBLG-PEG, were prepared and their aggregation structure and solubilization behaviors were investigated. These amphiphilic polypeptides were soluble in water to form spherical aggregates in which the hydrophobic alpha -helical peptide tail was orderly packed in the hexagonal manner. The solubilization of a plane solute, 1-naphthol, into these aggregates was characterized by semi- equilibrium dialysis (SED) method. Values of the solubilization equilibrium constant(K) decrease as the mole fraction of 1-naphthol in the aggregate (X) increases, And the solubilization isotherm of PBLG-PEG-1-naphthol system is higher as compared with that of PMLG-PEG-1-naphthol system. That is, the aromatic-aromatic interaction in the former system may enhance the solubilization affinity between the aggregate and solute. It is shown, therefore, that the interaction between peptide side chains and solutes is the effective factor to control the solubilization behavior of micellar aggregates composed of peptide-based amphiphiles. Thus, we can confirm the selective solubilization behaviors by the peptide- based orderly packed micelles in aqueous solutions, which may be a simple model system of our blood solutions containing albumin for their anomalous solubilization behaviors.
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