Multiple cellular and molecular substrates via redox and thiol–disulfide chemistry

Multiple cellular and molecular substrates via redox and thiol–disulfide chemistry describes a broad pharmacological mechanism where drugs interact with the cellular redox environment rather than a specific protein pocket (DrugBank, 2024). This mechanism is primarily associated with thiol-containing compounds like N-acetylcysteine (NAC) and Mesna, which act by donating electrons or participating in thiol-disulfide exchange reactions (PubMed, PMID: 30509180). In the context of mucolytics, these agents break disulfide bonds in mucin glycoproteins, thereby reducing mucus viscosity (StatPearls, 2023). Furthermore, this mechanism is essential for replenishing intracellular glutathione, the primary endogenous antioxidant, which neutralizes reactive oxygen species and toxic metabolites such as NAPQI in acetaminophen overdose (NIH, PubChem). Because the interaction is chemical and affects a wide array of substrates including enzymes, transcription factors, and structural proteins, it is classified as a non-specific systemic interaction (Journal of Biological Chemistry, 2018). Consequently, while therapeutically vital, it does not represent a single molecular target but rather a modulation of the collective thiolome (PubMed, PMID: 22503478).

Other names

ThiolomeRedoxomeThiol-disulfide exchange targetsRedox-active substrates

Reduction of disulfide bonds and scavenging of reactive oxygen species through thiol-disulfide exchange reactions.