Biomimetic Microdroplet Membrane Interface: Detection of the Lateral Localization of Amyloid Beta Peptides

Lateral membrane organization into domains, such as lipid rafts, plays an important role in the selective association of biological and nonbiological materials on heterogeneous membrane surfaces. The localization of such materials has profound influence on cellular responses. We constructed a biomimetic water-in-oil microdroplet membrane to study the lateral localization of these materials at heterogeneous biological interfaces. As a case study, we studied selective association of amyloid β peptide on the constructed membrane surface. Amyloid β peptide has attracted much attention as one of these membrane-associating proteins because of its “role” in Alzheimer’s disease pathology. Ternary lipid membranes covering microdroplets successfully produced lipid ordered structures, which mimicked biological lipid rafts. We revealed that amyloid β peptide selectively localizes within nonraft fluid membrane regions. The successful lateral organization in microdroplet membrane systems may lead to new opportunities for the study of molecular associations within heterogeneous membranes.