| Literature DB >> 34506798 |
Jun Hee Oh1, Jonggwan Park2, Yoonkyung Park3.
Abstract
Currently, multidrug-resistant bacteria are rapidly increasing worldwide because of the misuse or overuse of antibiotics. In particular, few options exist for treating infections caused by long-persisting oxacillin-resistant strains and recently proliferating carbapenem-resistant strains. Therefore, alternative treatments are urgently needed. The antimicrobial peptide (AMP) Lycosin-II is a peptide consisting of 21 amino acids isolated from the venom of the spider Lycosa singoriensis. Lycosin-II showed strong antibacterial activity and biofilm inhibition effects against gram-positive and gram-negative bacteria including oxacillin-resistant Staphylococcus aureus (S. aureus) and meropenem-resistant Pseudomonas aeruginosa (P. aeruginosa) isolated from patients. In addition, Lycosin-II was not cytotoxic against human foreskin fibroblast Hs27 or hemolytic against sheep red blood cells at the concentration of which exerted antibacterial activity. The mechanism of action of Lycosin-II involves binding to lipoteichoic acid and lipopolysaccharide of gram-positive and gram-negative bacterial membranes, respectively, to destroy the bacterial membrane. Moreover, Lycosin-II showed anti-inflammatory effects by inhibiting the expression of pro-inflammatory cytokines that are increased during bacterial infection in Hs27 cells. These results suggest that Lycosin-II can serve as a therapeutic agent against infections with multidrug-resistant strains.Entities:
Keywords: Anti-biofilm; Antimicrobial peptide; Mechanism of action; Pro-inflammatory cytokine; Pseudomonas aeruginosa; Staphylococcus aureus
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Year: 2021 PMID: 34506798 DOI: 10.1016/j.bbamem.2021.183769
Source DB: PubMed Journal: Biochim Biophys Acta Biomembr ISSN: 0005-2736 Impact factor: 3.747