Reactome | DCD peptide binds bacterial membrane phospholipids

DCD peptide binds bacterial membrane phospholipids

Stable Identifier

R-HSA-6803047

Type

Reaction [binding]

Species

Homo sapiens

Compartment

extracellular region, plasma membrane

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

DCD peptide binds bacterial membrane phospholipids

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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
23426625	Crystal structure and functional mechanism of a human antimicrobial membrane channel Song, C, Weichbrodt, C, Salnikov, ES, Dynowski, M, Forsberg, BO, Bechinger, B, Steinem, C, de Groot, BL, Zachariae, U, Zeth, K	Proc. Natl. Acad. Sci. U.S.A.	2013
20510021	Analysis of the solution structure of the human antibiotic peptide dermcidin and its interaction with phospholipid vesicles Jung, HH, Yang, ST, Sim, JY, Lee, S, Lee, JY, Kim, HH, Shin, SY, Kim, JI	BMB Rep	2010
22262861	Structure-activity analysis of the dermcidin-derived peptide DCD-1L, an anionic antimicrobial peptide present in human sweat 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	J. Biol. Chem.	2012
22455996	The multiple facets of dermcidin in cell survival and host defense Schittek, B	J Innate Immun	2012