Hinnavin I, an antibacterial peptide from cabbage butterfly, Artogeia rapae.
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Resumo
We have previously isolated four antibacterial peptides from the immune haemolymph of the fifth instar larvae of cabbage butterfly, Artogeia rapae [Yoe, S. M., Bang, I. S., Kang, C. S., and Kim, H. J. (1996) Mol. Cells 6, 609-614]. They were induced by live, nonpathogenic gram negative bacteria. One of these novel antibacterial peptides was named hinnavin I. Hinnavin I is heat stable; its activity was retained after 60 min incubation at 100 degrees C, being effective against gram negative and/or gram positive bacteria. Hinnavin I and lysozyme II showed a powerful synergistic effect on the inhibition of bacterial growth. Amino acid composition was analyzed and the molecular weight was determined to be 4,139.94+/-10.91 Da by the ESI mass spectrometer. To elucidate the primary structure of hinnavin I, the amino acid sequence of this peptide was determined by N-terminal sequencing techniques. The amino-terminal half of the molecule was rich in charged amino acids and was hydrophilic, whereas the carboxyl-terminal half was hydrophobic.