Identification and Characterization of an Antibacterial Peptide of the 26-kDa Protease of Sarcophaga peregrina with Antibacterial Activity.

J-STAGE
  • Tsuji Yumiko
    Graduate School of Pharmaceutical Sciences. The University of Tokyo
  • Aoyama Tomohisa
    Graduate School of Pharmaceutical Sciences. The University of Tokyo
  • Takeuchi Koh
    Graduate School of Pharmaceutical Sciences. The University of Tokyo
  • Homma Ko-ichi
    Graduate School of Pharmaceutical Sciences. The University of Tokyo
  • Takahashi Hideo
    Graduate School of Pharmaceutical Sciences. The University of Tokyo
  • Nakajima Yuki
    Natori Special Laboratory, The Institute of Physical and Chemical Research (RIKEN)
  • Shimada Ichio
    Graduate School of Pharmaceutical Sciences. The University of Tokyo
  • Natori Shunji
    Natori Special Laboratory, The Institute of Physical and Chemical Research (RIKEN)

抄録

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 phospholipids in the bacterial membranes.

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