Anoplin, a novel antimicrobial peptide from the venom of the solitary wasp Anoplius samariensis

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Konno, K.
Hisada, M.
Fontana, R.
Lorenzi, CCB
Naoki, H.
Itagaki, Y.
Miwa, A.
Kawai, N.
Nakata, Y.
Yasuhara, T.
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Elsevier B.V.
A novel antimicrobial peptide, anoplin, was purified from the venom of the solitary wasp Anoplius samariensis. The sequence was mostly analyzed by mass spectrometry, which was corroborated by solid-phase synthesis. Anoplin, composed of 10 amino acid residues, Gly-Leu-Leu-Lys-Arg-Ile-Lys-Thr-Leu-Leu-NH2, has a high homology to crabrolin and mastoparan-X, the mast cell degranulating peptides from social wasp venoms, and, therefore, can be predicted to adopt an amphipathic alpha -helix secondary structure. In fact, the circular dichroism. (CD) spectra of anoplin in the presence of trifluoroethanol or sodium dodecyl sulfate showed a high content, up to 55% of the alpha -helical conformation. A modeling study of anoplin based on its homology to mastoparan-X supported the CD results. Biological evaluation using the synthetic peptide revealed that this peptide exhibited potent activity in stimulating degranulation from rat peritoneal mast cells and broad-spectrum antimicrobial activity against both Gram-positive and Gram-negative bacteria. Therefore, this is the first antimicrobial component to be found in the solitary wasp venom and it may play a key role in preventing potential infection by microorganisms during prey consumption by their larvae. Moreover, this peptide is the smallest among the linear alpha -helical antimicrobial peptides hitherto found in nature, which is advantageous for chemical manipulation and medical application. (C) 2001 Elsevier B.V. B.V. All rights reserved.
anoplin, antimicrobial peptide, amphipathic alpha-helical structure, solitary wasp venom
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Biochimica Et Biophysica Acta-protein Structure and Molecular Enzymology. Amsterdam: Elsevier B.V., v. 1550, n. 1, p. 70-80, 2001.