モデルペプチドを用いたグループ3LEAタンパク質の乾燥誘導ガラス化の研究

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We studied thermodynamic properties of the following three different model peptides after desiccation in pure states and in binary ones with trehalose added: 1) model peptide (Hereafter referred to as PvLEA22), which consists of 2 repeats of the 11-mer consensus motif characteristic of late embryogenesis abundant proteins from P. vanderplanki, 2) model peptide designed as the two repeating sequence of PvLEA22 (Hereafter PvLEA44), and 3) control, i.e. the peptide with the amino acid composition identical with that of PvLEA22, although its sequence is randomized. Differential scanning calorimetry (DSC) measurements exhibited that all of the three peptides were vitrified in dried states at ambient temperature, although the glassy matrix of PvLEA22 in itself was found, by enthalpy relaxation rate, to be thermodynamically more stable than that of control. Two binary mixtures, PvLEA22: trehalose and control: trehalose, were analyzed by spectroscopic measurements (FT-IR) in temperature-dependent manners, with the conclusion that the glassy matrix of trehalose was strengthened by addition of the model peptides, of which effect was larger for PvLEA22 than for control.
2010-03-15