Self-assembly of a membrane protein governed by the fluctuation of the anchor peptide and the self-organization.

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Information on the fluctuation of protein is important to elucidate the function of the penetration of proteins on the biomembrane.The interaction between phospholipid and melitin molecules as a mode pepetide was evaluated by the mass spectorometery for the liposome. As a result, the relationship between the permeability of melitin through the membrane and the temperature was well fitted by the Arrhenisu law. These experimental results suggest that melitin molecules enhances the instability of the lipid membrane due to the higher permeability which is related to the specific chemical structure.