Potent broad-spectrum antibacterial peptide against both Gram-positive (B.subtilis, S.epidermidis, and S.aureus) and Gram-negative bacteria (E.coli, S.typhimurium, and P.aeruginosa) (PubMed:20721297, PubMed:23137439). Is also active against all antibiotic-resistant bacterial strains tested (PubMed:23137439). Induces apoptosis in C.albicans, but does not disrupt the fungal plasma membrane at all (PubMed:22542795). Acts by permeabilizing the bacterial cell membrane, but not human membranes (PubMed:23137439). Also shows potent anti-inflammatory activities, since it reduces both LPS-induced nitric oxide release and pro-inflammatory cytokine production (PubMed:23137439). Anti-inflammatory activities are initiated by suppressing the binding of LPS to toll-like receptor 4 (TLR4), and subsequently inhibiting the phosphorylation of p38 mitogen-activated protein kinase (MAPK) and nuclear translocation of NF-kB (TNFRSF11A) (PubMed:23137439). Does not show hemolytic activity against human erythrocytes (PubMed:23137439). Up-regulated from 4 hours after E.coli bacteria injection and higher expression level is reached at 16 hours. Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta) (PubMed:23137439). The alpha-helix is amphipathic (PubMed:23137439). Coprisin-derivatives (such as CopA3, and dCopW3) may be used as potent antibiotic therapeutic agent, or in treatment against tumors. The nonamer peptide CopA3 exhibits potent antibacterial activities (MIC=4-8 ug/mL) against both E.coli and S.aureus. This peptide (LLCIALRKK-NH2) is shorter than the mature peptide, amidated and with a Leu at position 60 instead of a His residue. Belongs to the invertebrate defensin family. Type 1 subfamily. Several experiments have been done with an amidated coprisin, although the amide donor for C-terminal amidation (usually a Gly residue) is missing in the precursor sequence.