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Antimicrobial Peptides intermediate

PGLa

Amphibian antimicrobial peptide from Xenopus laevis that synergizes with magainin 2 for enhanced membrane disruption.

By Encyclopeptide Editorial | 2 min read
antimicrobial-peptide amphibian synergy alpha-helical

Chemical Identity

PropertyValue
Chemical FormulaC90H155N23O20
Molecular Weight1855 Da
Peptide ClassAmphibian Antimicrobial Peptide
SequenceGMASKAGAIAGKIAKVALKAL-NH2
OriginXenopus laevis (African clawed frog)

Structure

PGLa (peptidyl-glycine-leucine-amide) is a 21-amino acid amphipathic alpha-helical peptide from Xenopus laevis skin. It is amidated at the C-terminus, enhancing membrane interaction. The peptide adopts a tilted helix orientation in lipid bilayers, and its activity is dramatically enhanced by synergy with magainin 2.

Mechanism of Action

PGLa disrupts bacterial membranes through its amphipathic alpha-helical structure. Uniquely, it shows strong synergy with magainin 2: the two peptides form heterodimers that insert more deeply into membranes, creating larger pores than either peptide alone. This synergy can increase activity 10-100-fold.

Clinical Applications

  • Research model: Studying AMP synergy and membrane mechanisms
  • Combination therapy potential: Synergistic formulations
  • Structure-activity studies: Understanding alpha-helical AMP mechanisms
  • Agricultural applications: Plant protection

Pharmacology

  • Spectrum: Broad (gram-positive, gram-negative)
  • Synergy: 10-100x potentiation with magainin 2
  • Membrane orientation: Tilted (30-40 degrees from normal)
  • Selectivity: Bacterial over mammalian membranes

References

  • Hoffman, W., et al. (1985). PGLa: a novel antimicrobial peptide from Xenopus skin. FEBS Letters, 190, 317-321.
  • Matsuzaki, K., et al. (1998). Synergy of PGLa and magainin 2. Biochemistry, 37, 15144-15153.

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