Inhibition of oxLDL binding requires CD36, but not other scavenger receptors. Binding of 125I-oxLDL was measured in wild type, Cd36-/- or Cd36/Sra-/- macrophages in the presence or absence of 20 μM Aβ to assess the role of CD36 and CD36/SRA-independent pathways. In the absence of CD36, oxLDL binding was not reduced by Aβ, indicating that this receptor is the target of Aβ inhibition. Binding of oxLDL via other scavenger receptors, which is measurable in Cd36/Sra-/- macrophages, was not inhibited by Aβ. Data are representative of triplicate samples ± standard deviation, *p ≤ 0.005.