ERp46 Inhibitors

ERp46 inhibitors encompass a diverse range of chemicals that indirectly modulate the function and activity of ERp46, a protein disulfide isomerase essential in protein folding within the endoplasmic reticulum (ER). These compounds primarily target the ER environment and related cellular processes, affecting ERp46's ability to assist in proper protein folding. For instance, Tunicamycin and Brefeldin A disrupt N-linked glycosylation and ER-Golgi transport, respectively, leading to ER stress which can subsequently influence ERp46 activity. Similarly, Thapsigargin, by inhibiting the SERCA pump, creates a stressful environment in the ER, impacting the protein folding capacity, including that of ERp46. Other inhibitors, such as Dithiothreitol (DTT) and β-Mercaptoethanol, act as reducing agents, disrupting the formation of disulfide bonds, a process central to ERp46's function. Compounds like Phenylarsine Oxide and Cadmium Chloride, known for binding to dithiols and inducing oxidative stress, respectively, can also affect the enzymatic activity of ERp46 by altering the redox state within the ER. N-Ethylmaleimide and Iodoacetamide, which alkylate sulfhydryl groups, have the potential to modify the protein folding environment, thus impacting ERp46. Furthermore, agents like Sodium 4-Phenylbutyrate and Curcumin, which act as chemical chaperones and modulators of various cellular pathways, can also influence ERp46's activity by modulating ER stress and the overall protein folding process.