Bactrocerin-1: A novel inducible antimicrobial peptide from pupae of oriental fruit flyBactrocera dorsalisHendel
| Autor: | Jin-Huan Tian, Jun Ishibashi, Ai Asaoka, Minoru Yamakawa, Shuo-Yang Wen, Yang Cao, Yi-Feng Li, Xiang-Li Dang, Wanying Yang, Hui-Yu Yi, Wen-Xian Wang |
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| Rok vydání: | 2009 |
| Předmět: |
Physiology
Molecular Sequence Data Lysine Peptide Microbial Sensitivity Tests Gram-Positive Bacteria Biochemistry Bactrocera dorsalis Mice Anti-Infective Agents Gram-Negative Bacteria Animals Amino Acid Sequence Peptide sequence chemistry.chemical_classification Sequence Homology Amino Acid biology Circular Dichroism Tephritidae Fungi General Medicine biology.organism_classification Antimicrobial Amino acid chemistry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Insect Science Insect Proteins Electrophoresis Polyacrylamide Gel Isoleucine Bacteria |
| Zdroj: | Archives of Insect Biochemistry and Physiology. 71:117-129 |
| ISSN: | 1520-6327 0739-4462 |
| DOI: | 10.1002/arch.20308 |
| Popis: | 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-NH(2)) 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 microM. Analysis of the Helical-wheel projection and the CD spectrum suggested that Bactrocerin-1 contains the amphipathic alpha-helix. |
| Databáze: | OpenAIRE |
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