Molecular characterization of a novel hepcidin (HepcD) from Camelus dromedarius. Synthetic peptide forms exhibit antibacterial activity.
J Pept Sci
; 20(9): 680-8, 2014 Sep.
Article
en En
| MEDLINE
| ID: mdl-24895313
Hepcidin is a cysteine-rich peptide widely characterized in immunological processes and antimicrobial activity in several vertebrate species. Obviously, this hormone plays a central role in the regulation of systemic iron homeostasis. However, its role in camelids' immune response and whether it is involved in antibacterial immunity have not yet been proven. In this study, we characterized the Arabian camel hepcidin nucleotide sequence with an open reading frame of 252 bp encoding an 83-amino acid preprohepcidin peptide. Eight cysteine key residues conserved in all mammalian hepcidin sequences were identified. The model structure analysis of hepcidin-25 peptide showed a high homology structure and sequence identity to the human hepcidin. Two different hepcidin-25 analogs manually synthesized by SPPS shared significant cytotoxic capacity toward the Gram-negative bacterium Escherichia coli American Type Culture Collection (ATCC) 8739 as well as the Gram-positive bacteria Bacillus subtilis ATCC 11779 and Staphylococcus aureus ATCC 6538 in vitro. The three disulfide bridges hepcidin analog demonstrated bactericidal activity, against B. subtilis ATCC 11779 and S. aureus ATCC 6538 strains, at the concentration of 15 µM (50 µg/ml) or above at pH 6.2. This result correlates with the revealed structural features suggesting that camel hepcidin is proposed to be involved in antibacterial process of innate immune response.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Bacterias
/
Hepcidinas
/
Antibacterianos
Límite:
Animals
/
Humans
Idioma:
En
Revista:
J Pept Sci
Asunto de la revista:
BIOQUIMICA
Año:
2014
Tipo del documento:
Article
País de afiliación:
Túnez
Pais de publicación:
Reino Unido