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The lipid membrane has been shown to mediate the fibrillogenesis and toxicity of Alzheimer's disease (AD) amyloid‐β (Aβ) peptide. Electrostatic interactions between Aβ40 and the phospholipid headgroup have been found to control the association and insertion of monomeric Aβ into lipid monolayers, where Aβ exhibited enhanced interactions with charged lipids compared with zwitterionic lipids. To elucidate the molecular‐scale structural details of Aβ‐membrane association, we have used complementary X‐ray and neutron scattering techniques (grazing‐incidence X‐ray diffraction, X‐ray reflectivity, and neutron reflectivity) in this study to investigate in situ the association of Aβ with lipid monolayers composed of either the anionic lipid 1,2‐dipalmitoyl‐sn‐glycero‐3‐[phospho‐rac‐(1‐glycerol)] (DPPG), the zwitterionic lipid 1,2‐dipalmitoyl‐sn‐glycero‐3‐phosphocholine (DPPC), or the cationic lipid 1,2‐dipalmitoyl …