Open AccessIn vitro activity of the antimicrobial peptides h-Lf1-11, MSI-78, LL-37, fengycin 2B, and magainin-2 against clinically important bacteria
Author(s) -
Laura Bedin Denardi,
Priscila de Arruda Trindade,
Carla Weiblen,
Lara Baccarin Ianiski,
Paula Cristina Stibbe,
Stefania Campos Pinto,
Jânio Morais Santúrio
Publication year - 2021
Publication title -
brazilian journal of microbiology
Language(s) - English
Resource type - Journals
eISSN - 1678-4405
pISSN - 1517-8382
DOI - 10.1007/s42770-021-00645-6
Subject(s) - magainin , microbiology and biotechnology , antimicrobial , acinetobacter baumannii , antibacterial activity , broth microdilution , staphylococcus aureus , pseudomonas aeruginosa , minimum inhibitory concentration , chemistry , bacteria , klebsiella pneumoniae , antimicrobial peptides , escherichia coli , biology , biochemistry , genetics , gene
We investigated the antibacterial activity of the antimicrobial peptides h-Lf1-11, MSI-78, LL-37, fengycin 2B, and magainin-2. The minimum inhibitory concentration (MIC) was determined by microdilution technique according to CLSI (M07-A9, 2012) against Escherichia coli, methicillin-resistant Staphylococcus aureus, Pseudomonas aeruginosa, carbapenem-resistant Klebsiella pneumoniae, and Acinetobacter baumannii. The MSI-78 showed potent bactericidal activity with MIC range of 1.25-40 mg/L against all bacterial strains. The h-Lf1-11, magainin-2, and LL-37 exhibited moderate activity (MIC range of 40-160, 80-160, and 40-160 mg/L, respectively) while the fengycin 2B did not show significant activity against all bacterial strains tested. These results revealed that MSI-78, h-Lf1-11, magainin-2, and LL-37 have great potential as antibacterial agents and their activity deserves to be more explored in further studies for the treatment of antibiotic-resistant bacteria.