Melittin-induced changes of the macroscopic structure of phosphatidylethanolamines
The binding of melittin to phosphatidylethanolamine model systems and its influence on the supramolecular organization of the lipid were investigated with binding assays, differential scanning calorimetry, /sup 31/P NMR, freeze-fracture electron microscopy, and small-angle X-ray scattering. The results are compared with binding to an analogous phosphatidylcholine and structural consequences thereof. Melittin binds with similar affinity to both lipid types in the liquid-crystalline state; at gel-phase temperatures, in contrast, interaction with phosphatidylethanolmaine is much weaker and does not lead to the bilayer fragmentation observed for phosphatidylcholines. With regard to phosphatidylethanolamine polymorphism, it is shown that melittin acts as an inhibitor of H/sub II/-phase formation and as a stabilizer of the bilayer organization. It is demonstrated that the remarkable variety of effects of melittin on the polymorphism of different membrane phospholipids can be understood in a relatively simple concept, taking into account the relative position and the shape of the interacting components
- Research Organization:
- State Univ. Utrecht (Netherlands)
- OSTI ID:
- 5238126
- Journal Information:
- Biochemistry; (United States), Vol. 27:7
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
PEPTIDES
CONFIGURATION INTERACTION
PHOSPHOLIPIDS
NUCLEAR MAGNETIC RESONANCE
X-RAY DIFFRACTION
AMINES
BIOCHEMISTRY
ELECTRON MICROSCOPY
PHOSPHORUS 31
CHEMISTRY
COHERENT SCATTERING
DIFFRACTION
ESTERS
ISOTOPES
LIGHT NUCLEI
LIPIDS
MAGNETIC RESONANCE
MICROSCOPY
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
ORGANIC PHOSPHORUS COMPOUNDS
PHOSPHORUS ISOTOPES
PROTEINS
RESONANCE
SCATTERING
STABLE ISOTOPES
550601* - Medicine- Unsealed Radionuclides in Diagnostics