design and evaluation of a novel anti-microbial peptide from cathelicidin-2: selectively active against <i>acinetobacter baumannii</i>

Background: infections caused by pathogenic microorganisms have increased the need for hospital care and have thus represented a public health problem and a significant financial burden. classical treatments consisting of traditional antibiotics face several challenges today. anti-microbial peptides (amps) are a conserved characteristic of the innate immune response among different animal species to defend against pathogenic microorganisms. objectives: in this study, a new peptide sequence (mchtl131-140) was designed using the in silico approach. methods: cathelicidin-2 (uniprotid: q2ial7) was used as a potential antimicrobial protein, and a novel 10 - 12 amino acids sequence amp was designed using bioinformatics tools and the amp databases. then, the anti-bacterial, anti-biofilm, and anti-fungal properties of the peptide, as well as its hemolytic activity and cytotoxicity towards human fibroblast (hdf) cells, were investigated in vitro. results: online bioinformatics tools indicated that the peptide sequence could have anti-bacterial, anti-viral, anti-fungal, and anti-biofilm properties with little hemolytic properties. the experimental tests confirmed that mchtl131-140 exhibited the best anti-bacterial properties against acinetobacter baumanniiand had fair anti-fungal properties. besides, it did not cause red blood cell lysis and showed no cytotoxicity towards hdf cells. conclusions: in general, the designed peptide can be considered a promising amp to control hospital-acquired infections by a. baumannii.