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Characteristics of the interaction of melittin with sarcoplasmic reticulum membranes

E A Shorina1, N V Mast, K B Storey

  • 1Department of Biochemistry, School of Biology, Lomonosov Moscow State University, Moscow, 119899, Russia. amr@atpase.bio.msu.su

Biochemistry. Biokhimiia
|July 9, 1999
PubMed

Insights

Bee venom peptide melittin rapidly binds to sarcoplasmic reticulum (SR) membranes, causing structural changes. Melittin induces slow aggregation of Ca-ATPase protein and alters the lipid bilayer viscosity and surface potential.

Area of Science:

  • Biochemistry
  • Biophysics
  • Membrane Biology

Background:

  • Sarcoplasmic reticulum (SR) vesicles are crucial for muscle contraction.
  • Melittin, an amphipathic peptide from bee venom, interacts with biological membranes.

Purpose of the Study:

  • To investigate the effects of melittin on the structure and function of SR membranes.
  • To elucidate the molecular mechanisms underlying melittin-induced changes in SR.

Main Methods:

  • Fluorescence spectroscopy to study melittin-SR complex.
  • Electron paramagnetic resonance (EPR) spectroscopy to probe membrane viscosity.
  • Surface potential measurements using neutral red dye.
  • Cross-linking assays to assess Ca-ATPase aggregation.

Main Results:

  • Melittin rapidly blue-shifted fluorescence and decreased intensity of the melittin-SR complex.
  • Melittin increased SR membrane viscosity and decreased surface potential.
  • Melittin induced slow aggregation of Ca-ATPase protein in SR membranes.

Conclusions:

  • Melittin rapidly binds to SR membranes.
  • Melittin induces slow conformational and oligomeric changes in Ca-ATPase.
  • Melittin causes structural transitions in the SR lipid bilayer.

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