Fragmentation of phospholipid bilayers by myelin basic protein
| Autor: | Myrna A. Monck, Frank A. Nezil, Michel Roux, Myer Bloom |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
biology
Lipid Bilayers Phospholipid Synthetic membrane Myelin Basic Protein Phosphatidylserines Phosphatidylserine Biochemistry Melittin Myelin basic protein Kinetics Structure-Activity Relationship chemistry.chemical_compound chemistry Phosphatidylcholine Phosphatidylcholines biology.protein Humans Calcium Fragmentation (cell biology) Lipid bilayer Protein Binding |
| Zdroj: | Biochemistry. 33:307-311 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi00167a040 |
| Popis: | Human myelin basic protein (MBP) is shown to disrupt multilamellar phosphatidylcholine bilayers into small lipoprotein particles in a manner similar to the cytolytic peptide melittin (Dufourc, E. J., Smith, I. C. P., & Dufourcq, J. (1986) Biochemistry 25, 6448-6455). This bilayer fragmentation, as monitored by 31P nuclear magnetic resonance, is temperature-dependent and completely inhibited by the presence of small amounts of negatively charged phosphatidylserine. The stabilizing property of phosphatidylserine is lost with the neutralization of its negative charges upon membrane binding of cationic species such as calcium ions. No MBP-induced fragmentation is observed with bilayers of negative or zwitterionic lipid mixtures which mimic the myelin lipid composition. The membrane fragmentation observed in vitro in the presence of MBP could play a role in vivo in demyelinating diseases. |
| Databáze: | OpenAIRE |
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