We isolated a novel monomeric peptide from antler plate polypeptide (APP-1) of sika deer which inhibited the growth of both Gram-positive and Gram-negative bacteria. The molecular mass and purity of this polypeptide was determined by ultra-performance liquid chromatography (UPLC) and Bruker micOTOF OllQ TOF mass spectrometry, respectively. The full amino-acid sequence of the monomericpeptide was analyzed by sequential Edman degradation using a protein/peptide sequencer. The antibacterial activity of the protein monomer in antlerplate was studied by disc diffusion method, and the antibacterial ring diameter of each antibacterial agent was measured to determine its antibacterial ability. The molecular mass and purity of this polypeptide was 18.970kDa and 90%. Amino acid sequence analyses indicated that the N-terminal amino-acid sequence of this monomeric peptide was AAQSLLACGAARLYKIIQQWPHYRR. The results showed that under the effect of various bacteriostatic agents, Enterobacter aeruginosa, Bacillus subtilis, Escherichia coli, Pseudomonas aeruginosa, Staphylococcus intermedius, Xylose staphylococcus all showed different degree of inhibitory effect. The inhibitory effect of the protein monomer on gram-positive bacteria was stronger than that on gram-negative bacteria, but not on candida albicans. This novel and monomeric APP-1 has antibacterial activities and imply that it is likely an important component of antibacterial activity in antler plate polypeptide.
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