The long-term objective of this research is to attain a better understanding of the structure of fibrils composed of fl-amyloid peptides. These fibrils are the main component of the senile plaques found in patients with Alzheimer's disease and have been implicated as the toxic species in that disease. It is hoped that a better understanding of the structure of these fibrils and the peptides of which they are composed will lead to preventative and therapeutic treatments for Alzheimer's disease. This project will initially focus on a model peptide before moving on to a subsection of the fl-amyloid peptide and, eventually, the complete peptide. The main technique for determining the structure of fl- amyloid will be solid-state nuclear magnetic resonance spectroscopy. The further development of this technique that will occur ill the course of this research project is likely to extend the applicability of solid-state nuclear magnetic resonance for structural determination of biological molecules.
| Loening, Nikolaus M; Chamberlin, Anne M; Zepeda, Andrea G et al. (2005) Quantification of phosphocholine and glycerophosphocholine with 31P edited 1H NMR spectroscopy. NMR Biomed 18:413-20 |
| Loening, Nikolaus M; Kanemitsu, Takuya; Seeberger, Peter H et al. (2004) Solid-phase synthesis and 1H and 13C high-resolution magic angle spinning NMR of 13C-labeled resin-bound saccharides. Magn Reson Chem 42:453-8 |
| Loening, Nikolaus M; Thrippleton, Michael J; Keeler, James et al. (2003) Single-scan longitudinal relaxation measurements in high-resolution NMR spectroscopy. J Magn Reson 164:321-8 |
| Loening, Nikolaus M; Rosay, Melanie; Weis, Volker et al. (2002) Solution-state dynamic nuclear polarization at high magnetic field. J Am Chem Soc 124:8808-9 |
