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- W2089185619 abstract "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 anti-microbial 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 µM. Analysis of the Helical-wheel projection and the CD spectrum suggested that Bactrocerin-1 contains the amphipathic α-helix. © 2009 Wiley Periodicals, Inc." @default.
- W2089185619 created "2016-06-24" @default.
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- W2089185619 date "2009-07-01" @default.
- W2089185619 modified "2023-09-30" @default.
- W2089185619 title "Bactrocerin-1: A novel inducible antimicrobial peptide from pupae of oriental fruit fly<i>Bactrocera dorsalis</i>Hendel" @default.
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- W2089185619 doi "https://doi.org/10.1002/arch.20308" @default.
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