Reactome | DCD peptide binds bacterial membrane phospholipids

DCD peptide binds bacterial membrane phospholipids

Stable Identifier

R-HSA-6803047

Type

Reaction

Species

Homo sapiens

Compartment

extracellular region, plasma membrane

Locations in the PathwayBrowser

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Summation

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	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	BMB Rep	2010
22262861	Structure-activity analysis of the dermcidin-derived peptide DCD-1L, an anionic antimicrobial peptide present in human sweat	J. Biol. Chem.	2012
22455996	The multiple facets of dermcidin in cell survival and host defense	J Innate Immun	2012

Participants

Input

Output

DCD:anionic phospholipid [extracellular region] (Homo sapiens)

Entity On Other Cell

Anionic phospholipids:microbial cell surface [plasma membrane]

Participant Of

hasEvent

Antimicrobial peptides

Authored

Shamovsky, Veronica, 2015-10-05

Reviewed

Hains, David S, 2016-08-02

Jupe, Steve, 2016-04-15