GrpEL2 Inhibitors

GrpEL2 Inhibitors primarily focus on impacting the pathways and processes that are associated with the function of GrpEL2, a co-chaperone that assists in mitochondrial protein folding. A major approach to this end involves targeting other chaperones, especially Hsp90. Compounds such as Geldanamycin, Radicicol, 17-AAG, and 17-DMAG are known Hsp90 inhibitors and can influence the protein folding and maturation processes, subsequently affecting GrpEL2 function.

Mitochondrial function and homeostasis are inherently linked to the role of GrpEL2. Thus, compounds like Concanamycin A, which inhibits V-ATPase, and Oligomycin, which inhibits mitochondrial ATP synthase, can indirectly impede the ATP-dependent processes of GrpEL2. Furthermore, the balance of protein synthesis and degradation is crucial for mitochondrial protein homeostasis. Compounds like Cycloheximide and Chloramphenicol, which affect protein synthesis, along with MG-132 and Bortezomib, proteasome inhibitors, can influence the protein equilibrium in mitochondria, indirectly implicating GrpEL2's function. Mito-TEMPO and Mdivi-1, by modulating mitochondrial oxidative stress and division respectively, offer another angle to indirectly affect GrpEL2's role in mitochondrial protein folding.