Bee venom-derived antimicrobial peptide melectin has broad-spectrum potency, cell selectivity, and salt-resistant properties

Sci Rep. 2020 Jun 23;10(1):10145. doi: 10.1038/s41598-020-66995-7.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids
  • Anti-Bacterial Agents*
  • Anti-Inflammatory Agents
  • Antimicrobial Cationic Peptides / chemistry
  • Antimicrobial Cationic Peptides / isolation & purification*
  • Antimicrobial Cationic Peptides / pharmacology*
  • Antimicrobial Cationic Peptides / toxicity
  • Bacteria / cytology
  • Bacteria / drug effects*
  • Bacterial Physiological Phenomena / drug effects
  • Bee Venoms / chemistry*
  • Cell Membrane / drug effects
  • Cells, Cultured
  • Drug Resistance, Bacterial
  • Fibroblasts / drug effects
  • Humans
  • Protein Binding
  • Protein Conformation, alpha-Helical
  • Salt Tolerance
  • Sodium Chloride
  • Static Electricity

Substances

  • Amino Acids
  • Anti-Bacterial Agents
  • Anti-Inflammatory Agents
  • Antimicrobial Cationic Peptides
  • Bee Venoms
  • melectin
  • Sodium Chloride