Late embryogenesis abundant (LEA) proteins are a highly diverse group of 
polypeptides expected to play important roles in desiccation tolerance of plant 
seeds. They are also found in other plant tissues and in some anhydrobotic 
invertebrates, fungi, protists and prokaryotes. The LEA protein LEAM accumulates 
in the matrix space of pea (Pisum sativum) mitochondria during late seed 
maturation. LEAM is an intrinsically disordered protein folding into amphipathic 
alpha-helix upon desiccation. This suggests that it could interact with the 
inner mitochondrial membrane, providing structural protection in dry seeds. 
Here, we have used Fourier-transform infrared and fluorescence spectroscopy to 
gain insight into the molecular details of interactions of LEAM with 
phospholipid bilayers in the dry state and their effects on liposome stability. 
LEAM interacted specifically with negatively charged phosphate groups in dry 
phospholipids, increasing fatty acyl chain mobility. This led to an enhanced 
stability of liposomes during drying and rehydration, but also upon freezing. 
Protection depended on phospholipid composition and was strongly enhanced in 
membranes containing the mitochondrial phospholipid cardiolipin. Collectively, 
the results provide strong evidence for a function of LEAM as a mitochondrial 
membrane protectant during desiccation and highlight the role of lipid 
composition in the interactions between LEA proteins and membranes.