Functional and structural characterization of recombinant dermcidin-1L, a human antimicrobial peptide.
Biochem Biophys Res Commun
; 328(1): 243-50, 2005 Mar 04.
Article
em En
| MEDLINE
| ID: mdl-15670776
ABSTRACT
Antimicrobial peptides from human skin are an important component of the innate immune response and play a key role as a first line of defense against infections. One such peptide is the recently discovered dermcidin-1L. To better understand its mechanism and to further investigate its antimicrobial spectrum, recombinant dermcidin-1L was expressed in Escherichia coli as a fusion protein and purified by affinity chromatography. The fusion protein was cleaved by factor Xa protease to produce recombinant dermcidin-1L. Antimicrobial and hemolytic assays demonstrated that dermcidin-1L displayed microbicidal activity against several opportunistic nosocomial pathogens, but no hemolytic activity against human erythrocytes even at concentrations up to 100 microM. Structural studies performed by circular dichroism spectroscopy indicated that the secondary structure of dermcidin-1L was very flexible, and both alpha-helix and beta-sheet structures might be required for the antimicrobial activity. Our results confirmed previous findings indicating that dermcidin-1L could have promising therapeutic potentials and shed new light on the structure-function relationship of dermcidin-1L.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Bactérias
/
Peptídeos Catiônicos Antimicrobianos
/
Hemólise
Limite:
Humans
Idioma:
En
Ano de publicação:
2005
Tipo de documento:
Article