<p>(<b>A</b>) Antibody binding curves against plate-immobilized PFs for SEC-isolated IVIg monomers (SEC Mon), dimers (SEC Dimer), and for Aβ-isolated IVIg IgGs with or without a 1:10 dilution of IgG-depleted normal human sera. Preparations of Aβ-isolated IVIg IgGs contained HMW, dimeric, and monomeric species (see <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0137344#pone.0137344.g003" target="_blank">Fig 3A</a>). (<b>B</b>) Bar charts for solution-phase PFs, monomeric Aβ and for non-amyloid molecules inhibition of IVIg IgG conformers binding to plate-immobilized PFs. Non-amyloid molecules were chosen based on their: 1) Abundance <i>in vivo</i> (extracellular matrix and elastin fibrils), 2) Association with polyreactive autoantibodies (DNA), 3) High hydrophobicity (maize protein zein), and 4) Non-amyloid aggregate state [amorphous aggregated carboxymethylated ovalbumin (CM-Oval)]. Competition studies were carried out using 0.1 mg/mL competitors and concentrations of IgG conformers that were equivalent to their EC<sub>50</sub> values for PFs: 400 nM IgG Monomers; 50 nM IgG dimers, and 20 nM Aβ-isolated IgGs. Each competition curve was carried out in duplicate, and bars represent the standard error. (<b>C</b>) IVIg IgG conformer binding curves against PFs and non-amyloid molecules, murine extracellular matrix gel (ECM) and human DNA.</p
