AlzheimersResearch
Curing Alzheimer's Disease
David J. E. Callaway, PhD
Professor and Laboratory Director
$$$$ "the Trillion-Dollar Disease" $$$$
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Biological NanoPhysics
Protein nanomachines are far more complex than any molecular machines that have yet been artificially constructed.
Their skillful utilization likely represents the future of medicine.
Our work clears significant hurdles to the use of this very important tool.
Dr Callaway has worked extensively in the field of Alzheimer's disease, specifically in understanding and controlling amyloid formation.
He has developed and patented several promising new therapeutics based upon apomorphine.
Potential therapeutics for Alzheimer's disease
Read the review on Wikipedia HERE
The polymerization of the amyloid beta-peptide into protease-resistant fibrils is a significant step in the pathogenesis of Alzheimer's disease. Compounds capable of interfering with the polymerization process thus may lead to potent therapeutics. In order to design such compounds, a detailed understanding of the polymerization process at the molecular level is essential. Conventional experimental techniques alone have lacked the precision to yield this detail. Accordingly, we employ a combination of biological, chemical, and physical techniques to understand and combat fibril formation.
Small-angle X-ray scattering
(SAXS)
with my
MILLION DOLLAR BABY
SANS/SAXS structure solving
Another recent publication HERE! and HERE! and HERE! and HERE! and HERE! and HERE!
New class of beta-amyloid aggregation inhibitors:
Implications for the mechanism of pathogenesis in Alzheimer's disease.
H. A. Lashuel, D. M. Hartley, D. Balakhaneh, A. Aggarwal, S. Teichberg, D.J.E. Callaway.
J. Biol. Chem., (2002) 277,42881-42890.
Assembling amyloid fibrils from designed structures containing a significant Alzheimer beta-peptide fragment.
L.O. Tjernberg, A. Tjernberg, N. Bark, Y. Shi, B. P. Ruzsicska, Z. Bu, J. Thyberg, D.J.E. Callaway.
Biochem. J. (2002) 366, 343-351.
Another recent publication HERE! and HERE!
Shi Y, Stouten PF, Pillalamarri N, Barile L, Rosal RV, Teichberg S, Bu Z, D.J.E. Callaway.
Quantitative determination of the topological propensities of amyloidogenic peptides.
Biophys Chem. 120 (2006), 55-61.
Bu Z, Shi Y, D.J.E. Callaway, {co-corresponding}, and Tycko R.
Molecular alignments within beta-sheets in Abeta(14-23) fibrils:
solid-state NMR experiments and theoretical predictions.
Biophys J. 2007 92: p. 594-602.
Another recent publication HERE!
Sengupta P, Garai K, Sahoo B, Shi Y, Callaway DJ, Maiti S.
The amyloid beta peptide (Abeta(1-40)) is thermodynamically soluble at physiological concentrations.
Biochemistry. 2003 Sep 9;42(35):10506-13.
Another recent publication HERE! and HERE!
Controlling amyloid beta-peptide fibril formation with protease stable ligands.
J. Biol. Chem. 1997 272 (19): 12601-12605; 272 (28): 17894.
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See research on ResearchGate, research on Academia●edu, research in high energy, nuclear, condensed matter and computational physics, research in biological nanophysics, research on Google Scholar, research on Mendeley, research on Scopus, profile on LinkedIn, profile on Wikipedia, mobility site, and Net Worth.
