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Dermcidin-1L 2KSG.png
Solution structure of dermcidin-1L.[1]
Available structures
PDB Ortholog search: PDBe, RCSB
External IDs OMIM606634 HomoloGene89039 GeneCards: DCD Gene
RNA expression pattern
PBB GE DCD gnf1h01261 at tn.png
More reference expression data
Species Human Mouse
Entrez 117159 n/a
Ensembl ENSG00000161634 n/a
UniProt P81605 n/a
RefSeq (mRNA) NM_001300854 n/a
RefSeq (protein) NP_001287783 n/a
Location (UCSC) Chr 12:
55.04 – 55.04 Mb
PubMed search [1] n/a

Dermcidin is a protein that in humans is encoded by the DCD gene,[2][3] and is an anti-microbial (antibiotic) peptide secreted by human eccrine sweat glands onto the skin as a part of the innate host defense of the immune system.


Dermcidin is a secreted protein that is subsequently processed into mature peptides of distinct biological activities. The C-terminal peptide is constitutively expressed in sweat and has antibacterial and antifungal activities. The N-terminal peptide, also known as diffusible survival evasion peptide, promotes neural cell survival under conditions of severe oxidative stress. A glycosylated form of the N-terminal peptide may be associated with cachexia (muscle wasting) in cancer patients.[3]

      Survival evasion peptide                            Antimicrobial peptide


The C-termial precursor DCD-1L is a 48 residue peptide that shows partial helicity in solution, as evidenced by the determination of its solution structure by NMR and CD-spectroscopy. The full length precursor is processed by undetermined proteases present in human sweat, to form several shorter peptides that show variable antimicrobial activity, named according to their C-terminal triplet of amino acids and their resiude length. One such active peptide is SSL25, which shows a 2-fold increase in activity against E.coli compared to DCD-1L.[4]



The crystal structure of dermcidin has been solved in solution to reveal a hexameric helix-bundle, mediated by Zn ion binding.[5] This is observed to form a tilted channel in membranes under computational examination by molecular dynamics simulations, and one suggested mechanism of antimicrobial action inferred from this observation is by ion gradient decoupling across biological membranes. This is supported by concurrent observations in experimental studies of a voltage dependent depolarization of lipid bilayers.


  1. ^ PDB 2KSG; Jung HH, Yang ST, Sim JY, Lee S, Lee JY, Kim HH, Shin SY, Kim JI (May 2010). "Analysis of the solution structure of the human antibiotic peptide dermcidin and its interaction with phospholipid vesicles". BMB Rep 43 (5): 362–8. doi:10.3858/bmbrep.2010.43.5.362. PMID 20510021. 
  2. ^ Schittek B, Hipfel R, Sauer B, Bauer J, Kalbacher H, Stevanovic S, Schirle M, Schroeder K, Blin N, Meier F, Rassner G, Garbe C (Nov 2001). "Dermicidin: a novel human antibiotic peptide secreted by sweat glands". Nat Immunol 2 (12): 1133–7. doi:10.1038/ni732. PMID 11694882. 
  3. ^ a b "Entrez Gene: DCD dermcidin". 
  4. ^ Baechle D, Flad T, Cansier A et al. (2006). "Cathepsin D is present in human eccrine sweat and involved in the postsecretory processing of the antimicrobial peptide DCD-1L.". J. Biol. Chem. 281 (9): 5406–15. doi:10.1074/jbc.M504670200. PMID 16354654. 
  5. ^ PDB 2YMKSong, Chen; Weichbrodt, Conrad; Salnikov, Evgeniy S; Dynowski, Marek; Forsberg, Björn O; Bechinger, Burkhard; Steinem, Claudia; de Groot, Bert L; Zachariae, Ulrich; Zeth, Kornelius (Feb 2013). "Crystal structure and functional mechanism of a human antimicrobial membrane channel". PNAS 110 (12): 4586–91. doi:10.1073/pnas.1214739110. PMID 23426625. 

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