グループ3LEAタンパク質のモデルペプチドによるリポソーム乾燥保護効果

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To investigate whether or not short model peptides work as substitutes for group-3 LEA (Late Embryogenesis Abundant) proteins, two peptides were tested: 1) PvLEA-22, which consists of two tandem repeats of the 11-mer motif characteristic to LEA proteins from an African sleeping chironomide, and 2) its control, i.e. the peptide with the amino acid composition identical with that of PvLEA-22, although its sequence is scrambled. Liposomes were prepared with DPPC (1,2-dipalmitoyl-sn-glycero-3-phosphocholine). Both of the two peptides were found to suppress the desiccation-induced aggregation of the liposome. When the liposome was dried in the presence of anyone of the two peptides, its gel-to-liquid crystalline temperature, measured by differential scanning calorimetry (DSC) and temperature-controlled Fourier transform infrared (FT-IR) spectroscopy, was lowered compared to that of the dried liposome without additives. The P=O stretching band (position was found to shift from that of the pure liposome in the dried state. The peptide secondary structure was composed of several different structures as well as α-helix in the dried peptide/liposome mixture, being different from the pure dried PvLEA-22, in which α-helix was predominant. These results are suggestive of the direct interactions between the added peptide and the membrane polar headgroup. Taken together, these two peptides are able to act as a kind of molecular shielding reagent by binding to the surfaces of the dried liposomes, and thereby to avoid their desiccation-induced damage.
低温生物工学会の論文
2012-10-15

グループ3LEAタンパク質のモデルペプチドによるリポソーム乾燥保護効果

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