科研之友
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摘要
A novel antimicrobial peptide, Bactrocerin-1, was purified and characterized from an immunized dipteran insect, Bactrocera, dorsalis. Bactrocerin-1 has 20 amino acid, residues with a mass of 2,325.95 Da. The amino acid, sequence of Bactrocerin-1 showed, very high. similarity to the active fragment (46V-65S-NH2) of Coleoptericin A. The composition of amino acid, residues revealed, that Bactrocerin-1 is a hydrophobic, positively charged, and Lys/Ile/Gly-rich peptide. Minimal growth inhibition concentration (MIC) measurements for synthesized Bactrocerin-1 showed a very broad spectrum, of antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria, and fungi. Bactrocerin-1 did. not show hemolytic activity toward mouse red blood. cells even at a concentration of 50 mu m. Analysis of the Helical-wheel projection and the CD spectrum suggested that. Bactrocerin-1 contains the amphipathic alpha-helix.
