Novel antimicrobial cecropins derived from O. curvicornis and D. satanas dung beetles

•The peptides satanin 1, 2, and curvicin are new Scarabaeidae cecropin from O. curvicornis and D. satanas.•Satanin 1, 2, and curvicin are cationic alpha helical antimicrobial peptides with low toxicity.•Satanin 1, 2, and curvicin inhibit the TNF-alpha production in LPS-stimulated PBMC.•Satanin 1 had in vitro antitumor activity against THP1 cells. Antibiotic resistance is an increasing global problem and therapeutic alternatives to traditional antibiotics are needed. Antimicrobial and host defense peptides represent an attractive source for new therapeutic strategies, given their wide range of activities including antimicrobial, antitumoral and immunomodulatory. Insects produce several families of these peptides, including cecropins. Herein, we characterized the sequence, structure, and biological activity of three cecropins called satanin 1, 2, and curvicin, found in the transcriptome of two dung beetle species Dichotomius satanas and Onthophagus curvicornis. Sequence and circular dichroism analyses show that they have typical features of the cecropin family: short length (38–39 amino acids), positive charge, and amphipathic α-helical structure. They are active mainly against Gram-negative bacteria (3.12–12.5 μg/mL), with low toxicity on eukaryotic cells resulting in high therapeutic indexes (TI > 30). Peptides also showed effects on TNFα production in LPS-stimulated PBMCs. The biological activity of Satanin 1, 2 and Curvicin makes them interesting leads for antimicrobial strategies.