个人简介

B.S., chemistry, Tsinghua University, Beijing, China, 2004 Ph.D., chemistry, Michigan State University, East Lansing, Michigan, 2009

研究领域

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.

近期论文

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W. Qiang*, R.D. Akinlolu, M. Nam, �Solid-state NMR studies of the membrane disruption induced by the b amyloid peptides: perspective and difficulties�, eMagRes (invited review), 2015, in press. W. Qiang*, W. M. Yau, and J. Schulte, �Fibrillation of b amyloid peptides in the presence of phospholipid bilayers and the consequent membrane disruption�, BBA-Biomembranes, 2015, 1848(1), 266-276. N.G. Sgourakis, W. M. Yau, and W. Qiang*, �Modeling an in-register, parallel Iowa Ab fibril structure using solid-state NMR data from labeled samples with Rosetta�, Structure, 2015, 23(1), 216-227. W. Qiang*, R.D. Akinlolu, M. Nam, and N. Shu, �Structural evolution and membrane interaction of the 40-residue b amyloid peptides: differences in the initial proximity between peptides and the membrane bilayer studied by solid-state nuclear magnetic resonance spectroscopy�, Biochemistry, 2014, 53(48), 7503-7514. W. Qiang, and R. Tycko, �Solid-state NMR studies of b-amyloid fibrils and related assemblies�, in Advances in Biological Solid-state NMR: Proteins and Membrane-Active Peptides, in press, A. Naito and F. Separovic, eds., Royal Society of Chemistry. J.X. Lu, W. Qiang, W.M. Yau, C.D. Schwieters, S.C. Meredith, and R. Tycko, �Molecular structure of b-amyloid fibrils in Alzheimer�s disease brain tissue�, Cell, 2013, 154(6), 1257-1268. C.M. Gabrys, W. Qiang, Y. Sun, L. Xie, S.D. Schmick, and D.P. Weliky, �Solid-state nuclear magnetic resonance measurements of HIV fusion peptide 13CO to lipid 31P proximities support similar partially inserted membrane locations of the a helical and b sheet peptide structures�, J. Phys. Chem. A., 2013, 117(39), 9848-9859. 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. K.N. Hu, W. Qiang, G. Bermejo, C.D.Schwieters, and R. Tycko, �Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N-15N and carbonyl 13C-13C dipolar recoupling data�, J. Magn. Reson., 2012, 218, 115-127. W. Qiang, W.M. Yau, Y. Luo, M.P. Mattson, and R. Tycko, �Antiparallel b-sheet architecture in Iowa-mutant b-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. K.N. Hu, W. Qiang, and R. Tycko, �A general Monte Carlo/simulated annealing algorithm for resonance assignment in NMR of uniformly labeled biopolymers�, J. Biomol. NMR, 2011, 50, 267-276. W. Qiang, W.M. Yau, and R. Tycko, �Structural evolution of Iowa-mutant b-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growth�, J. Am. Chem. Soc., 2011, 133, 4018-4029. S. Tristram-Nagle, R. Chan, E. Kooijman, P. Uppamoochikkal, W. Qiang, D.P. Weliky, and J.F. Nagle, �HIV fusion peptide penetrates, disorders, and softens T-cell membrane mimics�, J. Mol. Biol., 2010, 402, 139-153. C.M. Gabrys, R. Yang, C.M. Wasniewski, J. Yang, C.G. Canlas, W. Qiang, Y. Sun, and D.P. Weliky, �Nuclear magnetic resonance evidence for retention of lamellar membrane phase with curvature in the presence of large quantities of the HIV fusion peptide�, Biochim. Biophys. Acta, 2010, 1798, 194-201. 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. W. Qiang and D.P. Weliky, �HIV fusion peptide and its cross-linked oligomers: efficient syntheses, significance of the trimer in fusion activity, correlation of b strand conformation with membrane cholesterol, and proximity to lipid headgroups�, Biochemistry, 2009, 48, 289-301. W. Qiang, M.L.Bodner, and D.P. Weliky, �Solid-state NMR spectroscopy of HIV fusion peptides associated with host-cell-like membranes: 2D correlation spectra and distance measurements support a fully extended conformation and models for specific antiparallel strand registries�, J. Am. Chem. Soc., 2008, 130, 5459-5471. Z. Zheng, W. Qiang, and D.P. Weliky, �Investigation of finite-pulse radiofrequency-driven recoupling methods for measurement of intercarbonyl distances in polycrystalline and membrane-associated HIV fusion peptide samples�, Magn. Reson. Chem., 2007, 45, S247-S260.