Because amyloid proteins fold into various conformations and are generally disordered, it has been impossible to develop crystal structures to support rational drug design. Treventis scientists identified a common binding site based on epitope commonality between multiple misfolded amyloids. This information was used to build an experimentally validated model of the earliest stage of misfolding: a proprietary, patent-pending system known as “common conformational morphology” (CCM).

Using CCM, we can digitally screen, identify, and optimize numerous classes of potent, drug-like compounds before making and testing them experimentally – making structure-based design a reality for anti-amyloid drug discovery.