Dermcidin (DCD) is constitutively expressed in eccrine sweat glands, secreted into sweat and transported to the epidermal surface where it is proteolytically processed giving rise to several truncated DCD peptides (Schittek B et al. 2001; Rieg S et al. 2006). The processed forms such as the anionic DCD(63-110) (DCD-1L) and DCD(63-109) (DCD-1) possess antimicrobial activity against Gram-positive (Staphylococcus aureus, Enterococcus faecalis, Staphylococcus epidermidis, Listeria monocytogenes) and Gram-negative bacteria (Escherichia coli, Pseudomonas putida, Salmonella typhimurium) as well as Candida albicans (Cipakova I et al. 2006; Lai YP et al. 2005; Schittek B et al. 2001; Steffen H et al. 2006; Vuong C et al. 2004). The antimicrobial activity of DCD(63-110) (DCD-1L) is maintained over a broad pH range and at high salt concentrations that resemble the conditions in human sweat (Schittek B et al. 2001). DCD(63-110) was reported to interact with negatively charged bacterial phospholipids which lead to (Zn2+)-dependent formation of oligomeric complexes in the bacterial membrane, which subsequently lead to ion channel formation resulting in membrane depolarization and bacterial cell death (Paulmann M et al. 2012; Song C et al. 2013).