Proteins that misfold and cause disease are “intrinsically disordered”, meaning that they access many different conformations. This unique property has made it impossible to develop crystal structures to support rational drug design. Treventis scientists identified a common binding site based on epitope commonality between multiple misfolded proteins. This information was used to build an experimentally validated model of the earliest stage of misfolding: a proprietary, patented 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-misfolding drug discovery.