Abstract：
:A novel antimicrobial peptide (AMP) was identified from the centipede Scolopendra subspinipes mutilans by RNA sequencing, and the amino acid sequences predicted from the sequenced mRNAs were compared with those of known AMPs. We named this peptide scolopendin, according to its origin, and investigated the molecular mechanisms underlying its antimicrobial activity. Our findings showed that scolopendin had antimicrobial activity against several pathogenic microorganisms, but did not produce hemolysis of human erythrocytes. In addition, disturbances in the cell membrane potential, induction of potassium release from the cytosol, and increased membrane permeability of the microbes Candida albicans and Escherichia coli O157 were detected by the use of 3,3'-dipropylthiacarbocyanine iodide [DiSC3(5)] dye, potassium leakage assay, and propidium iodide influx assay, respectively, following scolopendin treatment. Further evidence to support the membrane-targeted action of scolopendin was obtained using artificial liposomes as models of the cell membrane. Use of calcein and FITC-labeled dextran leakage assays from scolopendin-treated giant unilamellar vesicles and large unilamellar vesicles showed that scolopendin has a pore-forming action on microbial membrane, with an estimated pore radius of 2.3-3.3 nm. In conclusion, scolopendin is a novel and potent AMP with a membrane-targeted mechanism of action.
journal_name
Biochimiejournal_title
Biochimieauthors
Lee W,Hwang JS,Lee DGdoi
10.1016/j.biochi.2015.08.015subject
Has Abstractpub_date
2015-11-01 00:00:00pages
176-84eissn
0300-9084issn
1638-6183pii
S0300-9084(15)00274-6journal_volume
118pub_type
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