Dermcidin-1L (human) . TFA

Dermcidin is an antimicrobial peptide constitutively expressed in sweat glands, secreted into the sweat and transported to the epidermal surface. In sweat it is proteolytically processed to Dermcidin-1L (DCD-1L) that has antimicrobial activity against a variety of pathogenic microorganisms and other peptides (e.g. DCD-1, Y-P30). Dermcidin-1L (DCD-1L) is a 48aa antimicrobial peptide (AMP) with a Leu residue on the C-terminus, secreted in sweat and part of the innate host defense of the immune system. Unlike most AMPs, which are cationic, DCD-1L has a net negative charge. DCD-1L displays antimicrobial activity thereby limiting skin infection by potential pathogens in the first few hours after bacterial colonization. Highly effective against E.coli, E.faecalis, S.aureus and C.albicans. DCD-1L is first monomeric in human sweat. DCD-1L interaction with negatively charged bacterial membrane phospholipids leads to Zn(2+) dependent formation of oligomeric DCD-1L complexes in the bacterial membrane, which subsequently leads to ion channel formation resulting in membrane depolarization and bacterial cell death. The gene products of DCD have been reported to be a neuronal survival factor, a putative oncogene in breast cancer and a proteolysis-inducing factor (PIF) that induces skeletal muscle proteolysis to cause cancer cachexia. Dermcidin protein function: DCD-1 displays antimicrobial activity thereby limiting skin infection by potential pathogens in the first few hours after bacterial colonization. Highly effective against E.coli, E.faecalis, S.aureus and C.albicans. Optimal pH and salt concentration resemble the conditions in sweat. Also exhibits proteolytic activity, cleaving on the C-terminal side of Arg and, to a lesser extent, Lys residues (PubMed:17448443). [The UniProt Consortium]