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J Microbiol Biotechnol ; 30(9): 1305-1309, 2020 Sep 28.
Artigo em Inglês | MEDLINE | ID: mdl-32627752

RESUMO

Insects possess biological defense systems that can effectively combat the invasion of external microorganisms and viruses, thereby supporting their survival in diverse environments. Antimicrobial peptides (AMPs) represent a fast-acting weapon against invading pathogens, including various bacterial or fungal strains. A 37-residue antimicrobial peptide, papiliocin, derived from the swallowtail butterfly Papilio xuthus larvae, showed significant antimicrobial activities against several human pathogenic bacterial and fungal strains. Jelleines, isolated as novel antibacterial peptides from the Royal Jelly (RJ) of bees, exhibit broad-spectrum protection against microbial infections. In this study, we developed a novel antimicrobial peptide, PAJE (RWKIFKKPFKISIHL-NH2), which is a hybrid peptide prepared by combining 1-7 amino acid residues (RWKIFKK-NH2) of papiliocin and 1-8 amino acid residues (PFKISIHL-NH2) of Jelleine-1 to alter length, charge distribution, net charge, volume, amphipaticity, and improve bacterial membrane interactions. This novel peptide exhibited increased hydrophobicity and net positive charge for binding effectively to the negatively charged membrane. PAJE demonstrated antimicrobial activity against both gram-negative and gram-positive bacteria, with very low toxicity to eukaryotic cells and an inexpensive process of synthesis. Collectively, these findings suggest that this novel peptide possesses great potential as an antimicrobial agent.


Assuntos
Antibacterianos/química , Antibacterianos/farmacologia , Peptídeos Catiônicos Antimicrobianos/química , Peptídeos Catiônicos Antimicrobianos/farmacologia , Borboletas/química , Sequência de Aminoácidos , Animais , Antibacterianos/síntese química , Peptídeos Catiônicos Antimicrobianos/síntese química , Bactérias/efeitos dos fármacos , Candida albicans/efeitos dos fármacos , Humanos , Interações Hidrofóbicas e Hidrofílicas , Larva/química , Testes de Sensibilidade Microbiana , Oligopeptídeos/química , Proteínas Recombinantes/síntese química , Proteínas Recombinantes/química , Proteínas Recombinantes/farmacologia
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