Proline conformation-dependent antimicrobial activity of a proline-rich histone h1 N-terminal Peptide fragment isolated from the skin mucus of Atlantic salmon.

ABSTRACT: A 30-residue N-terminally acetylated peptide derived from the N-terminal part of histone H1 was identified as the dominant antimicrobial peptide in skin mucus from Atlantic salmon (Salmo salar). The peptide (termed salmon antimicrobial peptide [SAMP H1]) was purified to homogeneity by a combination of reversed-phase and cation-exchange chromatographies. By Edman degradation of the deacetylated peptide and by sequencing of the PCR-amplified DNA that encodes the peptide, the complete amino acid sequence was determined to be AEVAPAPAAAAPAKAPKKKAAAKPKKAGPS. The theoretical molecular weight of N-terminally acetylated SAMP H1 was calculated to be 2,836, which is the same as that determined by matrix-assisted laser desorption ionization mass spectrometry. The peptide was active against both gram-

SUBMITTER: Luders T 

PROVIDER: S-EPMC1140541 | biostudies-literature | 2005 Jun

REPOSITORIES: biostudies-literature