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Published on: October 21, 2018
Prion protein-detergent micelle interactions studied by NMR in solution
Simone Hornemann1, Christine von Schroetter, Fred F Damberger
1Institute of Molecular Biology and Biophysics, ETH Zürich, 8093 Zürich, Switzerland. simone.hornemann@usz.ch
The Journal of Biological Chemistry
|June 24, 2009
Summary
Amino acid substitutions in cellular prion protein (PrP(C)) alter its interaction with cell membranes. These changes in membrane binding may influence PrP(C) function in health and transmissible spongiform encephalopathies.
Area of Science:
- Biochemistry
- Molecular Biology
- Neuroscience
Background:
- Cellular prion protein (PrP(C)) mutations are linked to increased susceptibility to human transmissible spongiform encephalopathies.
- PrP(C) is known to form transmembrane polypeptide segments.
Purpose of the Study:
- To investigate the interactions between dodecylphosphocholine micelles and recombinant mouse PrP variants with specific amino acid substitutions.
- To determine how these substitutions affect PrP(C) interaction with membranous structures.
Main Methods:
- Utilized recombinant mouse PrP variants with various amino acid replacements.
- Employed dodecylphosphocholine micelles to model membranous structures.
- Applied NMR chemical shift mapping to identify interaction sites.
Main Results:
- Wild-type mPrP-(90-231) and mPrP[M129V]-(91-231) showed weak interactions with micelles.
- Discrete interaction sites within the 102-127 polypeptide segment were identified for other PrP variants.
- Amino acid substitutions within residues 102-127 significantly affected PrP(C) interactions.
Conclusions:
- Amino acid substitutions in PrP(C) modulate its interaction with membranous structures.
- Altered membrane interactions may influence the physiological function of PrP(C) in health and disease.
- These findings provide insights into the molecular mechanisms underlying prion diseases.
