Assistant Professor, Biophysical Chemistry
My research interests focus on the biological application of solid state nuclear magnetic resonance (NMR) spectroscopy, with emphases on (1) understanding the physiological and molecular mechanisms of the neurotoxicity of β amyloid peptide associated with Alzheimer’s disease, (2) designing structural-specific amyloid bio bench markers and inhibitors for diagnostic and therapeutic applications, and (3) investigating the structure/function correlation of membrane penetrating peptides for anti-cancer treatment. We utilize other techniques in addition to the solid state NMR spectroscopy, including transmission electron microscopy, fluorescence spectroscopy, computational modeling as well as peptide and lipid chemistry.
J.X. Lu, W. Qiang, W.M. Yau, C.D. Schwieters, S.C. Meredith, and R. Tycko, “Molecular structure of β-amyloid fibrils in Alzheimer’s disease brain tissue”, Cell, 2013, 154(6), 1257- 1268.
W. Qiang, K. Kelley, and R. Tycko, “Polymorph-specific kinetics and thermodynamics of β- amyloid fibril growth”, J. Am. Chem. Soc., 2013, 135(18), 6860-6871.
W. Qiang, and R. Tycko, “Zero-quantum Stochastic Dipolar Recoupling in Solid State Nuclear Magnetic Resonance”, J. Chem. Phys., 2012, 137, 104201.
W. Qiang, W.M. Yau, Y. Luo, M.P. Mattson, and R. Tycko, “Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils”, Proc. Natl. Acad. Sci., 2012, 109, 4443-4448.
W. Qiang, “Signal enhancement for the sensitivity-limited solid state NMR experiments using a continuous, non-uniform acquisition scheme”, J. Magn. Reson., 2011, 213, 171-175.
W. Qiang, W.M. Yau, and R. Tycko, “Structural evolution of Iowa-mutant β-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growth”, J. Am. Chem. Soc., 2011, 133, 4018-4029.
W. Qiang, Y. Sun, and D.P. Weliky, “A strong correlation between fusogenicity and membrane insertion depth of the HIV fusion peptide”, Proc. Natl. Acad. Sci., 2009, 106, 15314-15319.
Last Updated: 1/28/14