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Biochem Biophys Res Commun. 2017 Dec 9;494(1-2):352-357. doi: 10.1016/j.bbrc.2017.10.019. Epub 2017 Oct 5.

A novel antimicrobial peptide isolated from centipede Scolopendra subspinipes mutilans stimulates neutrophil activity through formyl peptide receptor 2.

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Department of Biological Sciences, Sungkyunkwan University, Suwon 16419, Republic of Korea.
Department of Agricultural Biology, National Academy of Agricultural Science, RDA, Wanju 55365, Republic of Korea.
Department of Biological Sciences, Sungkyunkwan University, Suwon 16419, Republic of Korea; Department of Health Sciences and Technology, SAIHST, Sungkyunkwan University, Seoul 06351, Republic of Korea. Electronic address:


In this study, we identified scolopendrasin X, a novel antimicrobial peptide (AMP), from centipede Scolopendra subspinipes mutilans. Scolopendrasin X strongly stimulated mouse neutrophils, resulting in intracellular calcium increase, chemotactic migration through pertussis toxin-sensitive G-protein and phospholipase C pathway, and increased superoxide anion production in neutrophils. Target receptor for scolopendrasin X, formyl peptide receptor (FPR)2 mediated scolopendrasin X-induced neutrophil activation. Moreover, scolopendrasin X significantly blocked inflammatory cytokine production induced by lipopolysaccharide in mouse neutrophils. Taken together, our results suggest that the novel AMP scolopendrasin X can be used as a material to regulate neutrophil activity through FPR2.


Antimicrobial peptide; Chemotaxis; Formyl peptide receptor 2; Neutrophil; Scolopendra subspinipes mutilans; Superoxide anion

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