Formation of microdomains in cell membranes investigated by microscopic analyses of structures of membranes and proteins

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The monomeric amyloid・peptide (A ・・ binds to the phosphatidylcholine membrane in the lamellar gel phase but not in the liquid crystalline phase. Tightly packed phosphatidylcholine membranes appear to serve as a platform for non-electrostatic binding and self-association of A・. On the other hand, aggregated A・peptides bind to the phosphatidylcholine membrane both in the lamellar gel and the liquid crystalline phases. The binding of aggregated A・significantly reduces fluidity of the membrane in the liquid crystalline phase.