Journal
ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY
Volume 88, Issue 1, Pages 31-44Publisher
WILEY
DOI: 10.1002/arch.21193
Keywords
Cecropin A; antimicrobial peptide; anti-inflammatory peptide
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Funding
- Priority Research Centers Program [2009-0093824]
- Basic Science Research Program [2011-0022873, 2013R1A1A2058021]
- National Research Foundation of Korea [2009-0093824, 2013R1A1A2058021, 2014M3A9B8022854] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Cecropin A is a novel 37-residue cecropin-like antimicrobial peptide isolated from the cecropia moth, Hyalophora cecropia. We have demonstrated that cecropin A is an antibacterial agent and have investigated its mode of action. In this study, we show that cecropin A has potent antimicrobial activity against 2 multidrug resistant organismsAcinetobacter baumanii andPseudomonas aeruginosa. Interactions between cecropin A and membrane phospholipids were studied using tryptophan blue shift experiments. Cecropin A has a strong interaction with bacterial cell mimetic membranes. These results imply that cecropin A has selectivity for bacterial cells. To address the potential the rapeutic efficacy of cecropin A, its anti-inflammatory activities and mode of action in mouse macrophage-derived RAW264.7 cells stimulated with lipopolysaccharide (LPS) were examined. Cecropin A suppressed nitrite production, mTNF-, mIL-1, mMIP-1, and mMIP-2 cytokine release in LPS-stimulated RAW264.7 cells. Furthermore, cecropin A inhibited intracellular cell signaling via the ERK, JNK, and p38 MAPK pathway, leading to the prevention of COX-2 expression in LPS-stimulated RAW264.7 cells. These results strongly suggest that cecropin A should be investigated as a potential agent for the prevention and treatment of inflammatory diseases.
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