Scientific Reports · 2020 · 65 citations · 33 references
Life SciencesMicrobiologyPharmacologyAntimicrobial ResistanceDrug DiscoveryProtein BiochemistryAntibacterial AgentsAntibacterial PharmacologyAntimicrobial PeptidesPeptide ChemistryPeptide Drug DiscoveryVenom BiologyAmino AcidsAnti-inflammatory ActivityAnti-inflammatory ResponseAntibacterial PeptidesAntimicrobial Peptide ActivityCationic Antimicrobial PeptidesDrug-resistant PathogensPeptide Structure-activity Relationships
Antimicrobial peptides have attracted attention as alternatives to conventional antibiotics. Previously, a novel antimicrobial peptide, melectin, consisting of 18 amino acids was isolated from the venom of a bee, Melecta albifrons. Here, we investigated the antibacterial activity of melectin against drug-resistant bacteria. Melectin showed broad-spectrum antimicrobial activity but low cytotoxicity and no hemolytic activity. Melectin maintained its antimicrobial activity at physiological salt concentrations. Melectin is an α-helical structure that binds to the bacterial membrane via electrostatic interactions and kills bacteria in a short time by bacterial membrane targeting. Collectively, our results suggest that melectin has antibacterial activity and anti-inflammatory activity.
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