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