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Cecropin D‐like antibacterial peptides from the sphingid moth, Agrius convolvuli
Author(s) -
Lee In Hee,
Chang Keun Young,
Choi Chung Sik,
Kim Hak R.
Publication year - 1999
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/(sici)1520-6327(1999)41:4<178::aid-arch2>3.0.co;2-w
Subject(s) - biology , cecropin , antibacterial peptide , microbiology and biotechnology , botany , peptide , antibacterial activity , bacteria , antimicrobial peptides , biochemistry , genetics
Two major antibacterial peptides were isolated and purified from immunized larval hemolymph of Agrius convolvuli . Acid extraction, gel filtration, ultrafiltration, and reversed‐phase FPLC were used for purification of peptides. These peptides had similar molecular mass and amino acid composition. Moreover, 21 of the first 23 N terminal residues were identical. The peptides were highly homologous with cecropin D in size and primary sequence, and named Agrius cecropin D1 and D2. The molecular masses of Agrius cecropin D1 and D2 were 3,879.39 and 3,839.27, respectively. In antibacterial and hemolytic assays, Agrius cecropin D showed potent antibacterial activities against a panel of Gram positive and negative bacteria without hemolytic activity against human red blood cells. Notably, our antibacterial assay revealed Agrius cecropin D possessed stronger or at least equivalent activities against B. megaterium than cecropin A. It suggests that Agrius cecropin D, which has an alternative structure from cecropin D, could be the model for the development of peptide antibiotics. Arch. Insect Biochem. Physiol. 41:178–185, 1999. © 1999 Wiley‐Liss, Inc.