Background
Wei Qiang's research applies the biological solid-state nuclear magnetic resonance (NMR) spectroscopy and other biophysical, biochemistry and cell biology approaches to understand the mechanisms of b-amyloid-aggregation-induced neuronal cell toxicity and cell death.
Current projects include:
- Understanding the molecular and structural basis of non-specific membrane disruption along the process of b-amyloid aggregation. This project uses mainly solid-state NMR approaches to explore the structural and dynamic features of intermediate states in the process of membrane-associated amyloidosis.
- Exploring the amyloid structural polymorphisms and cell disruption induced by the post-translational modified b-amyloid peptide variants. This project applies solid-state NMR spectroscopy, microscopy approaches and cell-based quantitative analysis.
Accepting BCCB graduate students
Select Publications
- Heterotypic Interactions Between the 40- and 42-Residue Isoforms of b-Amyloid Peptides on Lipid Bilayer Surfaces
- Modulation of Aggregation and Structural Polymorphisms of b-Amyloid Fibrils in Cellular Environments by Pyroglutamate-3 Variants Cross-Seeding (2023) L. Cruceta, Y. Sun, J.M. Kenyaga, D. Ostrovsky, A. Rodgers, L. Vugmeyster, L. Yao, W. Qiang. J. Biol. Chem., 299, 10, 105196.
- In-Cell 31P Solid-State NMR Measurements of the Lipid Dynamics and Influence of Exogenous Beta-Amyloid Peptides on Live Neuroblastoma Neuro-2a Cells. (2023) J. Kenyaga, S.A. Otieno, W. Qiang. Biophys. Chem., 297, 107008.
- Early-Stage b-Amyloid-Membrane Interactions Modulate Lipid Dynamics and Influence Structural Interface and Fibrillation. (2022) J. Kenyaga, Q. Cheng, W. Qiang,
- Cross-seeded Fibrillation Induced by Pyroglutamate-3 and Truncated A尾40 Variants Leads to A尾40 Structural Polymorphism Modulation and Elevated Toxicity. (2021) Z.W. Hu, L. Cruceta, S. Zhang, Y. Sun, W. Qiang. ACS Chem. Neurosci., 12, 3625-3637.
Education
- Ph.D. Michigan State University
- B.S. Tsinghua University, China
Research Interests
- Biological solid-state nuclear magnetic resonance spectroscopy
- Membrane biophysics
- Structural biology of amyloid aggregates