Date published: 2025-10-12

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REG3α Inhibitors

REG3α inhibitors represent a chemical class of compounds that specifically target and inhibit the activity of the protein Regenerating islet-derived protein 3 alpha (REG3α), a member of the C-type lectin family. REG3α is known for its role in binding carbohydrate structures, particularly peptidoglycan components, which makes it integral to interactions with bacterial cell walls. Structurally, REG3α contains a carbohydrate recognition domain (CRD) characteristic of C-type lectins, which facilitates its interaction with polysaccharides. Inhibitors of REG3α, therefore, are typically designed to disrupt this interaction, often by targeting the lectin-like domain or the critical residues involved in sugar binding. These inhibitors might also affect conformational changes in REG3α or interfere with its oligomerization, which can be essential for its function.

The design of REG3α inhibitors often involves detailed studies of the protein's crystal structure to identify key binding pockets and residues that can be exploited. For instance, molecular docking studies are frequently employed to simulate how potential inhibitors interact with REG3α's carbohydrate-binding groove. Chemical scaffolds for these inhibitors might range from small organic molecules that fit into the lectin-binding site to larger compounds that block critical protein-protein interactions or alter REG3α's overall structure. The specificity of these inhibitors is vital, as REG3α shares structural similarities with other members of the Reg family and C-type lectins. This requires careful optimization to avoid off-target interactions with similar proteins. The development of REG3α inhibitors also involves understanding their physicochemical properties, such as solubility, binding affinity, and stability, which are critical for achieving effective inhibition of REG3α activity in various chemical environments.

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