Abstract
Cytoplasmic granules of neutrophils store a variety of cationic polypeptides, which exert in vitro a potent antibacterial action and are potentially involved in host defense mechanisms. From an acid extract of bovine neutrophil granules we have purified over 2,000-fold a dodecapeptide exhibiting bactericidal activity against both Escherichia coli and Staphylococcus aureus at 10(-7)-10(-5) M concentration. The purification procedure involved only two steps of ion-exchange and reversed-phase chromatography. The peptide, named bactenecin, has the amino acid sequence, Arg-Leu-Cys-Arg-Ile-Val-Val-Ile-Arg-Val-Cys-Arg, maintained in a cyclic structure by a disulfide bond between the two cysteine residues. Computer modeling of the dodecapeptide resulted in a conformation in which the chain adopts an antiparallel extended structure forming a gamma turn at residue 7.
Keywords
AntibioticsMicrobiologyChemistryBiology
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Publication Info
- Year
- 1988
- Type
- article
- Volume
- 263
- Issue
- 20
- Pages
- 9573-9575
- Citations
- 275
- Access
- Closed
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Cite This
D Romeo,
Barbara Skerlavaj,
Martino Bolognesi
et al.
(1988).
Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils..
Journal of Biological Chemistry
, 263
(20)
, 9573-9575.
https://doi.org/10.1016/s0021-9258(19)81553-3
Identifiers
- DOI
- 10.1016/s0021-9258(19)81553-3