ChMAP-28 was predicted bioinformatically based on the sequence data of the precursor protein MAP-28 (GenBank AJ243126.1). The ChMAP-28 amino acid sequence was translated from mRNA for the corresponding precursor protein as a 27-residue peptide without the C-terminal glycine, a common amidation signal in cathelicidins. It has molecular mass of 3365 Da and the amino acid sequence GRFKRFRKKLKRLWHKVGPFVGPILHY including eleven basic residues. The goat peptide is highly homologous to the bovine α-helical cathelicidin BMAP-27. ChMAP-28 was found to be toxic toward tumor cells at concentrations of <10 μM, significantly less toxic toward normal cells and low hemolytic. The cytotoxic effect of ChMAP-28 is revealed in 15 min and does not increase during following incubation. Its cell death promoting mechanism was not associated with the caspase-dependent apoptosis, but was rather related to necrosis due to pore formation in the susceptible cell membranes.