Hinnavin I, an antibacterial peptide from cabbage butterfly, Artogeia rapae

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.