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Melectin: A Novel Antimicrobial Peptide from the Venom of the Cleptoparasitic Bee Melecta albifrons
Author(s) -
Čeřovský Václav,
Hovorka Oldřich,
Cvačka Josef,
Voburka Zdeněk,
Bednárová Lucie,
Borovičková Lenka,
Slaninová Jiřina,
Fučík Vladimír
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200800476
Subject(s) - venom , bee venom , peptide , antimicrobial , antimicrobial peptides , antibacterial peptide , microbiology and biotechnology , biology , chemistry , zoology , ecology , biochemistry , bacteria , antibacterial activity , genetics
A novel antimicrobial peptide designated melectin was isolated from the venom of the cleptoparasitic bee Melecta albifrons . Its primary sequence was established as H‐Gly‐Phe‐Leu‐Ser‐Ile‐Leu‐Lys‐Lys‐Val‐Leu‐Pro‐Lys‐Val‐Met‐Ala‐His‐Met‐Lys‐NH 2 by Edman degradation and ESI‐QTOF mass spectrometry. Synthetic melectin exhibited antimicrobial activity against both Gram‐positive and ‐negative bacteria and it degranulated rat peritoneal mast cells, but its hemolytic activity was low. The CD spectra of melectin measured in the presence of trifluoroethanol and sodium dodecyl sulfate showed a high content α‐helices, which indicates that melectin can adopt an amphipathic α‐helical secondary structure in an anisotropic environment such as the bacterial cell membrane. To envisage the role of the proline residue located in the middle of the peptide chain on biological activity and secondary structure, we prepared several melectin analogues in which the Pro11 residue was either replaced by other amino acid residues or was omitted. The results of biological testing suggest that a Pro kink in the α‐helical structure of melectin plays an important role in selectivity for bacterial cells. In addition, a series of N‐ and C‐terminal‐shortened analogues was synthesized to examine which region of the peptide is related to antimicrobial activity.