ISPD Inhibitors

ISPD inhibitors, as a class, consist of chemicals that indirectly affect the function of ISPD by influencing the pathways and processes it is involved in. ISPD is known for its role in the biosynthesis of CDP-ribitol, which is necessary for the glycosylation of alpha-dystroglycan. Disruption of glycosylation-related processes might therefore impact ISPD activity. The inhibitors target various stages of the glycosylation pathway, from the initial steps in the endoplasmic reticulum to the later modifications in the Golgi apparatus.

These inhibitors work by interfering with enzymes that catalyze the addition of sugar moieties to proteins and lipids, an essential process for proper cellular function. For instance, Tunicamycin inhibits the formation of N-glycosidic linkages, which could lead to a decrease in overall glycosylation, thereby affecting the environment in which ISPD operates. Swainsonine and castanospermine target specific glycosidase enzymes, altering the glycosylation pattern that might intersect with ISPD's function. Deoxynojirimycin and deoxymannojirimycin specifically inhibit different glucosidases and mannosidases, respectively, which are pivotal in processing glycoproteins that could be substrates of ISPD.