Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach
David B Teplow, Noel D Lazo, Gal Bitan, Summer Bernstein, Thomas Wyttenbach, Michael T Bowers, Andrij Baumketner, Joan-Emma Shea, Brigita Urbanc, Luis Cruz, …
Accounts of chemical research, v 39(9), pp 635-645
Amino Acid Sequence Thermodynamics Models, Molecular Molecular Sequence Data Protein Conformation Amyloid beta-Peptides - chemistry Protein Folding
Oligomeric, neurotoxic amyloid protein assemblies are thought to be causative agents in Alzheimer's and other neurodegenerative diseases. Development of oligomer-specific therapeutic agents requires a mechanistic understanding of the oligomerization process. This is a daunting task because amyloidogenic protein oligomers often are metastable and comprise structurally heterogeneous populations in equilibrium with monomers and fibrils. A single methodological approach cannot elucidate the entire protein assembly process. An integrated multidisciplinary program is required. We discuss here the synergistic application of in hydro, in vacuo, and in silico methods to the study of the amyloid beta-protein, the key pathogenetic agent in Alzheimer's disease.
Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach
Creators
David B Teplow -
Department of Neurology, David Geffen School of Medicine, Brain Research Institute, and Molecular Biology Institute, University of California, Los Angeles, California 90095, USA. dteplow@ucla.edu
Noel D Lazo
Gal Bitan
Summer Bernstein
Thomas Wyttenbach
Michael T Bowers
Andrij Baumketner
Joan-Emma Shea
Brigita Urbanc
Luis Cruz
Jose Borreguero
H Eugene Stanley
Publication Details
Accounts of chemical research, v 39(9), pp 635-645