Crystals of a bapineuzumab-Aβ complex may explain how the antibody targets amyloid plaques in the brain, according to researchers in Australia. In the February 18 Scientific Reports, Michael Parker and colleagues at St. Vincent's Institute of Medical Research, Melbourne, report that bapineuzumab, a humanized mouse antibody, captures the N-terminal of Aβ in a helical conformation. This interaction may be unique. In complexes with mouse antibodies, which are used preclinically, the Aβ N-terminal exists as a random coil without secondary structure. "The thing that distinguishes bapineuzumab from the non-clinical N-terminal antibodies is that it recognizes a conformation-dependent epitope.