Dr. Wei Qiang
Assistant Professor, Biophysical Chemistry
- B.S., chemistry, Tsinghua University, Beijing, China, 2004
- Ph.D., chemistry, Michigan State University, East Lansing, Michigan, 2009
- Science 2 Bldg - Room B28B
- Group web page:
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.
S.Z. Hanz, N.S. Shu, J. Qian, N. Christman, P. Kranz, M. An, C. Grewer, and W. Qiang, "Protonation-driven membrane insertion of the pH-low insertion peptide", Angew. Chem. Int. Ed., 2016, in press.
D.A. Delgado, K.E. Doherty, Q. Cheng, H. Kim, D. Xu, H. Dong, C. Grewer, and W. Qiang, "Distinct membrane disruption pathways induced by the 40-residue beta-amyloid peptides", J. Biol. Chem., 2016, 291(23), 12233-44.
N.S. Shu, M. S. Chung, L. Yao, M. An, and W. Qiang, "Residue-specific structures and membrane locations of pH-low insertion peptide by solid-state nuclear magnetic resonance", Nat. Commun., 2015, 6, 7787.
R.D. Akinlolu, M. Nam, and W. Qiang, "Competition between fibrillation and induction of vesicle fusion for the membrane-associated 40-residue beta-amyloid peptide", Biochemistry, 2015, 54, 3416-19. - Highlighted on Biochemistry Webpage.
N. Sgourakis, W.M. Yau, and W. Qiang*, "Modeling an in-register, parallel "Iowa" Abeta fibril structure using solid-state NMR data from sparsely labeled samples with Rosetta", Structure, 2015, 23, 216-27 .
W. Qiang, W.M. Yau, and J. Schulte, "Fibrillation of beta amyloid peptides in the presence of phospholipid bilayers and the consequent membrane disruption", BBA-Biomembranes, 2015, 1848, 266-76.
W. Qiang, R.D. Akinlolu, M. Nam, and N.S. Shu, "Structural evolution and membrane interaction of the 40-residue beta-amyloid peptide: differences in the initial proximity between peptides and the membrane bilayer studied by solid-state nuclear magnetic resonance spectroscopy", Biochemistry, 2014, 53, 7503-14.