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Membrane fusion induced by 11-mer anionic and cationic peptides: a structure-function study

E I Pecheur1, I Martin, J M Ruysschaert

  • 1Department of Physiological Chemistry, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands. e.pecheur-huet@med.rug.nl

Biochemistry
|March 28, 1998
PubMed
Summary

Subtle sequence changes in fusogenic peptides significantly alter their membrane interaction and fusion capabilities. Peptide structure, not just helicity, is crucial for controlled liposome fusion and minimal leakage.

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Area of Science:

  • Biochemistry
  • Membrane Biophysics
  • Peptide Chemistry

Background:

  • Amphipathic peptides can induce membrane fusion.
  • Previous work showed an 11-amino acid peptide (WAE) promotes liposome fusion when anchored.
  • The relationship between peptide structure and fusogenic activity requires further investigation.

Purpose of the Study:

  • To investigate the relationship between peptide structure and fusogenic properties.
  • To test if specific structural motifs are required for WAE-induced fusion.
  • To compare the fusion activity and membrane interaction of WAE with three analogues: WAK, WAEPro, and WAS.

Main Methods:

  • Synthesis and structural analysis (infrared attenuated total reflection spectroscopy) of 11-mer peptides.
  • Assessment of liposome fusion activity and leakage using fluorescence assays.

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  • Investigation of peptide-membrane interaction via tryptophan fluorescence and iodide quenching.

    • Main Results:

    • All peptides adopted helical structures upon liposomal anchorage, but fusion outcomes varied.
    • WAE and WAK induced non-leaky fusion, while WAEPro and WAS caused significant leakage.
    • WAE and WAK peptides showed partial Trp residue penetration into membranes, unlike WAEPro and WAS.

    Conclusions:

    • Peptide helicity alone is insufficient for optimal fusogenic properties.
    • Subtle primary sequence differences dictate peptide-membrane interaction modes (surface vs. penetration).
    • Sequence specificity plays a critical role in WAE-induced liposome fusion and its functional outcomes.