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Whey-Derived Antimicrobial Anionic Peptide Interaction with Model Membranes and Cells.

Melania M Noe1,2,3, Jésica A Rodríguez4,5, Gabriela R Barredo Vacchelli4,5

  • 1Departamento de Química, Catedra de Química Biológica, Facultad de Ciencias Exactas, Físicas y Naturales, Universidad Nacional de Córdoba, Córdoba 5000, Argentina.

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This study reveals how the antimicrobial peptide beta-lactoglobulin (β-lg)125-135 interacts with model cell membranes. The peptide preferentially targets and alters bacterial membranes over eukaryotic ones, suggesting a mechanism for its antimicrobial action.

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Area of Science:

  • Biochemistry
  • Membrane Biophysics
  • Antimicrobial Peptides

Background:

  • Antimicrobial peptides are crucial in host defense and represent a promising alternative to conventional antibiotics.
  • Understanding the precise mechanisms of antimicrobial peptide-host cell membrane interactions is vital for developing new therapeutic agents.
  • Beta-lactoglobulin (β-lg) is a major milk protein with potential antimicrobial properties, particularly after hydrolysis.

Purpose of the Study:

  • To elucidate the interaction mechanism of the anionic antimicrobial peptide β-lg125-135 with model eukaryotic (dpPC) and bacterial (dpPC:dpPG) membranes.
  • To investigate how the peptide's charge and membrane composition influence its adsorption, penetration, and membrane perturbation.
  • To confirm the peptide's bactericidal activity and safety on eukaryotic cells.

Main Methods:

  • Surface pressure measurements and compression isotherms of lipid monolayers (dpPC and dpPC:dpPG) exposed to β-lg125-135.
  • Fluorescence anisotropy (FA) assays using DPH and TMA-DPM probes in small unilamellar vesicles (SUVs) of dpPC and dpPC:dpPG.
  • Confirmation of antimicrobial activity against Gram-positive bacteria and cytotoxicity assessment on a eukaryotic cell line.

Main Results:

  • β-lg125-135 showed increased penetration and adsorption to negatively charged dpPC:dpPG monolayers compared to zwitterionic dpPC.
  • The peptide exhibited higher adsorption/desorption rates and a lower association constant with dpPC:dpPG, indicating transient interactions.
  • Monolayers containing β-lg125-135 showed altered surface properties, including decreased compressibility and increased surface potential, especially on dpPC:dpPG.
  • In SUVs, β-lg125-135 disrupted dpPC bilayers but increased anisotropy in dpPC:dpPG bilayers, suggesting membrane stiffening.

Conclusions:

  • β-lg125-135 demonstrates a strong preference for negatively charged (bacterial) membrane interfaces due to electrostatic attraction.
  • The peptide's interaction with bacterial membranes is characterized by favorable orientation but low stability and residence time.
  • The peptide effectively stiffens bacterial model membranes, contributing to its proposed mechanism of antimicrobial action.