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).
Paulmann, M, Arnold, T, Linke, D, Özdirekcan, S, Kopp, A, Gutsmann, T, Kalbacher, H, Wanke, I, Schuenemann, VJ, Habeck, M, Bürck, J, Ulrich, AS, Schittek, B
Song, C, Weichbrodt, C, Salnikov, ES, Dynowski, M, Forsberg, BO, Bechinger, B, Steinem, C, de Groot, BL, Zachariae, U, Zeth, K
Burian, M, Schittek, B
© 2020 Reactome
