Journal
JOURNAL OF BIOCHEMISTRY
Volume 130, Issue 2, Pages 313-318Publisher
JAPANESE BIOCHEMICAL SOC
DOI: 10.1093/oxfordjournals.jbchem.a002988
Keywords
amphiphilic alpha-helix; antibacterial peptide; bacterial membrane; insect; serine protease
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Previously, we purified a serine protease with a molecular mass of 26 kDa that exhibits potent antibacterial activity from a pupal extract of Sarcophaga peregrina (flesh fly). We divided this protease into 12 peptides and examined their antibacterial activity. A peptide corresponding to residues 155 to 174 (peptide 9) was found to exhibit antibacterial activity comparable to that of the 26-kDa protease. When Escherichia coli was treated with peptide 9, the permeability of both the outer and inner membranes increased, and substrates for beta -lactamase and beta -galactosidase entered the cells, but beta -galactosidase did not leak out of the cells under these conditions. It was suggested that residues 6 to 18 of peptide 9 form an amphiphilic a-helix under hydrophobic conditions with an N-terminal basic loop and then interact with acidic phospholipids in the bacterial membranes.
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