Protein Disulfide Isomerases & Heat Shock Proteins

Protein disulfide-isomerase (PDI) is a multifunctional enzyme and chaperone in the endoplasmic reticulum that catalyzes the formation, rearrangement, and reduction of disulfide bonds during the folding of secretory and membrane proteins; it plays key roles in ER protein quality control, antigen presentation, and the unfolded protein response[1][3][4][5]. Heat shock proteins (HSPs) are a large family of molecular chaperones that stabilize, refold, and prevent aggregation of misfolded proteins under stress conditions, participating in cell survival, immunity, inflammation, and disease modulation[5][7][10].

Other names

PDIPDIA1EC 5.3.4.1HspHsp70Hsp90Chaperone

PDI inhibitors: Inhibit disulfide bond formation/isomerization, disrupt protein folding, induce ER stress/apoptosis. HSP inhibitors: Block chaperone function, destabilize oncogenic client proteins, modulate immune response, induce apoptosis.