Dermcidin

Also known as: Preproteolysin, DCD, P81605

**Mechanism of Action** Dermcidin (DCD), also known as preproteolysin, is a 110-amino-acid peptide constitutively secreted by eccrine sweat glands into human sweat. Its active antimicrobial form, DCD-1L, is generated via proteolytic cleavage and exhibits broad-spectrum activity against bacteria (e.g., *Staphylococcus aureus*, *Escherichia coli*) and fungi. The mechanism involves membrane disruption through pore formation, facilitated by its amphipathic α-helical structure, which targets negatively charged microbial membranes without harming host cells. DCD also modulates innate immunity by acting as a chemoattractant for immune cells and promoting wound healing. **Key Research Findings** Preclinical studies demonstrate that DCD-1L retains antimicrobial activity under high-salt and acidic conditions typical of human sweat, distinguishing it from other antimicrobial peptides. Research has identified DCD expression in various tissues beyond sweat glands, including the brain and breast, suggesting pleiotropic roles. Experimental models show that DCD deficiency correlates with increased susceptibility to skin infections, while overexpression enhances bacterial clearance. Notably, DCD-derived fragments have been implicated in cancer cell survival (e.g., proteolysis-inducing factor in cachexia), though this remains under investigation. **Clinical Relevance** Dermcidin is in the experimental stage, with potential applications in topical antimicrobial therapies for chronic wounds, acne, and atopic dermatitis, where sweat-derived immunity is compromised. Its stability in physiological sweat makes it a candidate for infection-resistant biomaterials. However, clinical translation is limited by challenges in synthetic production and the need for safety profiling, particularly given its association with tumor progression in certain cancers. For research purposes only — not medical advice.

Key data

Mechanism of action

Found in sweat, has an antimicrobial activity during early bacterial colonization (PubMed:11694882, PubMed:23426625). The secreted peptide assembles into homohexameric complexes that can associate with and also insert into pathogen membranes (PubMed:23426625). Once inserted in bacteria membranes forms anion channels probably altering the transmembrane potential essential for bacterial survival (PubMed:23426625). Highly effective against E.coli, E.faecalis, S.aureus and C.albicans (PubMed:11694882). Optimal pH and salt concentration resemble the conditions in sweat (PubMed:11694882). Also exhibits proteolytic activity, cleaving on the C-terminal side of Arg and, to a lesser extent, Lys residues (PubMed:17448443)

Research & studies

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