DCD peptide binds bacterial membrane phospholipids

Stable Identifier
Reaction [binding]
Homo sapiens
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Dermcidin peptides, DCD1(63-109) and DCD-1L(63-110), are anionic peptides with a net negative charge of -2 at physiological pH (Paulmann M et al. 2012). Despite its negative net charge, DCD peptides possess an amphiphilic structure due to its cationic N-terminal region (Ser1 to Lys23) and its anionic C-terminal part (Asp24 to Leu48). The cationic N-terminal part is mainly responsible for the binding of DCD to the negatively charged phospholipids.
Literature References
PubMed ID Title Journal Year
20510021 Analysis of the solution structure of the human antibiotic peptide dermcidin and its interaction with phospholipid vesicles

Kim, HH, Kim, JI, Lee, JY, Yang, ST, Shin, SY, Jung, HH, Lee, S, Sim, JY

BMB Rep 2010
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
22455996 The multiple facets of dermcidin in cell survival and host defense

Schittek, B

J Innate Immun 2012
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