Casocidin-I: a casein-alpha s2 derived peptide exhibits antibacterial activity.
Here we report the isolation and characterization of an antibacterial peptide from bovine milk inhibiting the growth of Escherichia coli, and Staphylococcus carnosus. The primary structure of the peptide was revealed as a 39-amino-acid-containing fragment of bovine alpha s2-casein (position 165-203) by means of Edman amino acid sequencing and mass spectrometry. Since human milk does not contain any casein-alpha s2, these findings could explain the different influence of human and bovine milk on the gastrointestinal flora of the suckling.
Zucht
H D
HD
Niedersächsisches Institut für Peptid-Forschung (IPF) Hannover, Germany.
Raida
M
M
Adermann
K
K
Mägert
H J
HJ
Forssmann
W G
WG
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000302:isolation & purification*; D002364:Caseins / Q000737:chemistry* / Q000302:isolation & purification*; D002417:Cattle; D004926:Escherichia coli / Q000187:drug effects / Q000254:growth & development; D006801:Humans; D008892:Milk / Q000737:chemistry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification*; D013210:Staphylococcus / Q000187:drug effects / Q000254:growth & development
D000900:Anti-Bacterial Agents; D002364:Caseins; D010446:Peptide Fragments; C096060:casocidin I