Amyloid beta A4 peptide is found in the extracellular region of the senile plaque and in the angiopathy of Alzheimer's disease. Several other proteins, including IgG, also reside in these abnormal structures. In an attempt to understand how these structures are assembled and to determine how proteins are recruited, interactions of various proteins with synthetic beta A4 peptide have been examined in vitro. Purified IgG binds directly to synthetic beta A4 peptide with high avidity. The domain between amino acids 12-28 of beta A4 binds IgG. beta A4 peptide binds the hinge region of the immunoglobulin heavy chain, and preserves the ability of the immunoglobulin to bind antigen. A protein which does not bind directly to beta A4 peptide can be targetted to the senile plaque and angiopathy by binding to IgG, which avidly binds beta A4 peptide.