DCD forms oligomeric complex

Stable Identifier
Reaction [binding]
Homo sapiens
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DCD peptide is initially monomeric when secreted in human sweat. In presence of a negatively charged bacterial membrane the cationic N-terminus of DCD gets attracted electrostatically (Paulmann M et al. 2012). Upon interaction with the bacterial membrane a change in the secondary structure from random coil to an alpha-helical conformation is induced. DCD-1(L) self-assembles into a higher oligomeric state which is stabilized by zinc ions. Subsequently, by oligomerization DCD is able to form ion channels in the bacterial membrane resulting in bacterial cell death ( (Paulmann M et al. 2012; Song C et al. 2013; Burian M & Schittek B 2015).
Literature References
PubMed ID Title Journal Year
23426625 Crystal structure and functional mechanism of a human antimicrobial membrane channel

Zeth, K, de Groot, BL, Steinem, C, Zachariae, U, Bechinger, B, Salnikov, ES, Forsberg, BO, Weichbrodt, C, Dynowski, M, Song, C

Proc. Natl. Acad. Sci. U.S.A. 2013
22262861 Structure-activity analysis of the dermcidin-derived peptide DCD-1L, an anionic antimicrobial peptide present in human sweat

Bürck, J, Kalbacher, H, Paulmann, M, Arnold, T, Habeck, M, Wanke, I, Kopp, A, Özdirekcan, S, Schittek, B, Gutsmann, T, Linke, D, Ulrich, AS, Schuenemann, VJ

J. Biol. Chem. 2012
25596890 The secrets of dermcidin action

Burian, M, Schittek, B

Int. J. Med. Microbiol. 2015
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