抄録
Group 3 late embryogenesis abundant (G3LEA) proteins have repeating sequences composed of characteristic 11-mer motif and are likely to act as a protectant against desiccation-induced aggregation of proteins in anhydrobiotic organisms. However, its molecular mechanism remains unclear. In this study, we first show experimentally that a LEA-model peptide, composed of two repeats of the 11-mer motif, prevents the aggregation of lysozyme induced by desiccation. Next, to interpret this result at atomic level, we study the structure of the LEA-model and its interaction with lysozyme by means of both all-atom and coarse-grained molecular dynamics simulations. It is shown that the LEA model preferentially adopts a turn structure in water, but by addition of lysozyme its structure is transformed into an extended one to bind to the surface of lysozyme. In conclusion, the LEA-model can protect lysozyme from aggregation by shielding the protein surface to inhibit protein-protein direct contact.
