TBCB Inhibitors

Tubulin Folding Cofactor B (TBCB) inhibitors, as described in the context of this table, are not direct inhibitors in the classical sense, but rather compounds that can affect the function of TBCB by altering the dynamics of tubulin, the protein that TBCB helps to fold. TBCB is involved in the proper folding and functioning of tubulin subunits, which are the building blocks of microtubules. Compounds such as colchicine, vincristine, and paclitaxel are known to interact with tubulin and affect microtubule polymerization or depolymerization. Such interactions can inadvertently affect the role of TBCB, as the availability and conformational state of tubulin are critical for its function.

These compounds span a range of chemical classes, including alkaloids (e.g., colchicine and vincristine), taxanes (e.g., paclitaxel), and synthetic derivatives (e.g., eribulin). They can bind to distinct sites on tubulin or microtubules, leading to stabilization or destabilization of the microtubule structure. By altering the equilibrium between tubulin dimers and microtubules, these compounds can exert an indirect influence on TBCB. For example, stabilizing microtubules can prevent tubulin subunits from being available for proper folding by TBCB, while destabilizing agents can lead to an accumulation of tubulin dimers that may not be properly processed by TBCB. Although these compounds are not designed to target TBCB directly, their effects on tubulin and microtubule dynamics can result in an indirect modulation of TBCB's function within the cell.