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The secrets of dermcidin action
Burian, Marc ;
Schittek
, Birgit
International journal of medical microbiology, 2015-02, Vol.305 (2), p.283-286
[Periódico revisado por pares]
Germany: Elsevier GmbH
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Título:
The secrets of dermcidin action
Autor:
Burian, Marc
;
Schittek
, Birgit
Assuntos:
Animals
;
Antimicrobial Cationic Peptides - metabolism
;
Antimicrobial peptides
;
Bacteria - drug effects
;
Cell Membrane - metabolism
;
Dermcidin
;
Humans
;
Infectious Disease
;
Ion channel
;
Ion Channels - metabolism
;
Medical Education
;
Microbial Viability - drug effects
;
Oligomerization
;
Peptides - metabolism
;
Phospholipids - metabolism
;
Protein Multimerization
;
Staphylococcus aureus
É parte de:
International journal of medical microbiology, 2015-02, Vol.305 (2), p.283-286
Notas:
ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
Descrição:
Abstract Antimicrobial peptides (AMPs) are important effector molecules of the innate immune defense of diverse species. The majority of known AMPs are cationic therefore facilitating the initial binding of the positively charged peptides to the negatively charged bacterial membrane. Dermcidin (DCD) is constitutively expressed in eccrine sweat glands, secreted into sweat and transported to the epidermal surface where it is proteolytically processed giving rise to several truncated DCD peptides. Its processed forms such as the anionic 48mer DCD-1L and the 47mer DCD-1 possess antimicrobial activity against numerous bacteria including Staphylococcus aureus . Here, the latest knowledge regarding the mode of action of the anionic DCD-1(L) and the functional consequences of their interaction with bacterial membranes is reviewed. There is evidence that the interaction of DCD-1(L) with negatively charged bacterial phospholipids leads to Zn2+ dependent formation of oligomeric complexes in the bacterial membrane, which subsequently leads to ion channel formation resulting in membrane depolarization and bacterial cell death.
Editor:
Germany: Elsevier GmbH
Idioma:
Inglês
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