 This study examined the effectiveness of PITACs, a new type of drug designed to degrade specific proteins, by studying their interactions with two targets, SMARPA2 and BRD4. By analyzing the ternary complexes formed between these targets and PITACs, researchers were able to determine how the structural features of the PITACs affected their ability to bind to the targets and degrade them. They found that the more tightly bound the protac was to its target, the higher its degradation rate. This suggests that the size and shape of the PITACs can be used to optimize their degradative properties. Furthermore, they developed a computational model to estimate the amount of surface area of the ternary complex that is buried within the interface, which correlated well with the measured binding affinity. These results provide a framework for optimizing PITACs for maximum efficacy. This article was offered by Ryan P. Wurz, Won Rui, Ken Delamaja, and others. We are article.tv, links in the description below.