Journal Article

Identification and Characterization of an Antibacterial Peptide of the 26-kDa Protease of <i>Sarcophaga peregrina</i> with Antibacterial Activity

Yumiko Tsuji, Tomohisa Aoyama, Koh Takeuchi, Ko-ichi Homma, Hideo Takahashi, Yuki Nakajima, Ichio Shimada and Shunji Natori

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 130, issue 2, pages 313-318
Published in print August 2001 | ISSN: 0021-924X
Published online August 2001 | e-ISSN: 1756-2651 | DOI:
Identification and Characterization of an Antibacterial Peptide of the 26-kDa Protease of Sarcophaga peregrina with Antibacterial Activity

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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 β-lactamase and (β-galactosidase entered the cells, but β-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 α-helix under hydrophobic conditions with an N-terminal basic loop and then interact with acidic phosphoh'pids in the bacterial membranes.

Keywords: amphiphilic a-helix; antibacterial peptide; bacterial membrane; insect; serine protease

Journal Article.  0 words. 

Subjects: Biochemistry

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