Abstract
It is known that group 3 late embryogenesis abundant (G3LEA) proteins have the ability to protect membrane and proteins from desiccation stress. G3LEA proteins commonly have characteristic 11-mer repeat motif. In our previous studies using short model peptides for G3LEA proteins, we had already demonstrated that the 11-mer motif forms the core functional site of those proteins. However, the function of parts of non-repeat sequences remains unclear. Here we investigated the structure and function of the non-repeat regions using their 22-mer model peptides. The secondary structure of the peptides in solution and dry states were investigated by means of CD and FTIR spectroscopy. In addition, to test whether these peptides are able to protect liposome against drying-rehydration stress, we conducted particle size distribution measurements and fluorescence measurements. In conclusion, the non-repeat regions studied here take mainly β-sheet structure in the dry state, and have no apparent ability to protect liposome from the desiccation stress.
