Abstract
We investigated whether a model peptide for group 3 late embryogenesis abundant (G3LEA) proteins that we had developed previously is capable of protecting liposomes against their fusion under desiccation stress. Four different peptides were tested for comparison: 1) PvLEA-22, which consists of two tandem repeats of the 11-mer motif characteristic of LEA proteins from an African sleeping chironomid; 2) a peptide with amino acid composition identical to that of PvLEA-22, but with its sequence scrambled; 3) poly-L-glutamic acid; and 4) poly-L-lysine. Based upon the results of the particle size distribution measurement of liposomes and the leakage test of a fluorescent probe inside liposomes, we argue that the synthetic 22-mer peptide that derived from its parent G3LEA protein sequence is superior to simple homopeptides as the anti-fusion reagent of liposomes and can achieve the ability of protecting liposome that is comparable to or higher than several native LEA proteins reported previously.
