Keywordsfrog skin; magainin; PGLa; caerulein-precursor fragment; xenopsin-precursor-fragment; hymenochirin; tethered bilayer lipid membranes; self-assembled monolayers; electrochemical impedance spectroscopy; potential-step chronocoulometry; cyclic voltammetry; host defense peptides; antimicrobial resistance; antibiotic alternatives; chicken; antimicrobial peptide; insect defensin; lucifensin; maggot therapy; Lucilia sericata; Lucilia cuprina; peptide isolation; peptide identification; defensin; pleurocidin; cathelicidin; hepcidin; piscidin; Acinetobacter baumannii; antimicrobial peptides; Gram-negative pathogens; Pseudomonas aeruginosa; specificity determinant(s); temperature-profiling by RP-HPLC; antimicrobial chemokines; antimicrobial neuropeptides; antimicrobial proteins; cathelicidin LL-37; defensins; dermcidin; hepcidins; histatins; RNases; antimicrobial peptides; antibacterial; reptile; biofilm; broad-spectrum; Gram-positive; Gram-negative; peptide antibiotic; gene duplication; exon-intron structure; cysteine-stabilized α-helical and β-sheet motif; antimicrobial peptides; mechanism of action; peptidomimetics; plant antimicrobial peptides; cysteine-rich peptides; cystine knot; thionin; defensin; hevein; knottin
