In order for cells to function, they must be properly supported, having contacts with neighboring cells and/or the extracellular matrix  ECM). The ECM provides much of the structural support available to parenchymal cells in tissues. The primary proteins present in the ECM and indeed the entire body are the collagens, a family of proteins with at least 29 members. They share a common structural motif of helical fibrils formed by three protein subunits. Another cytoplasmic protein, β-Catenin, plays essential roles in two different cellular processes: calcium-dependent intercellular adhesion and Wnt-mediated transcriptional activation. For cell–cell adhesion, β-catenin binds the cytoplasmic domain of cadherin adhesion receptors along with the actin binding protein, α-catenin, to bridge the extracellular adhesive activity of cadherins with the underlying actin cytoskeleton. This cadherin-bound pool of β-catenin ultimately form the so-called adherens junctions and serves to link the cytoskeletal networks of adjacent cells, which is considered essential for normal tissue architecture and morphogenesis[1],[2].
Aggregation of extracellular amyloid-β (Aβ) is thought to play a major part in the pathogenesis of Alzheimer's disease. Amyloid plaques form when levels of the monomeric, soluble Aβ peptide build up in the extracellular interstitial fluid (ISF) in the brain. Caprospinol (Axon 1442) has the ability to bind Aβ42, prevent β-amyloid aggregation, and block the formation of Aβ42 oligomers, thereby protecting organisms against β-amyloid (Aβ42)-induced neurotoxicity[3].