Research | Mysite

top of page

This site was designed with the

website builder. Create your website today.Start Now

Research in Qiang Laboratory focuses on the biophysical and biochemical aspects of amyloid protein assemblies and membrane-associated proteins and peptides. Current projects study the molecular basis of Alzheimer's disease related pathological mechanisms and the membrane interactions of pH-sensitive drug-delivery peptides.

Molecular Basis of Cellular Membrane Disruptions Induced by the Amyloidogenic Aggregation of Beta-Amyloid Peptides

The project explores the key molecular structures of membrane-disrupting beta-amyloid aggregates and the crucial peptide-lipid interactions that lead to such membrane disruption processes. Sub-directions of the project include: (1) Characterizations of the membrane-associated beta-amyloid fibril structures; (2) Characterizations of the membrane-stabilized beta-amyloid oligomer structures; (3) Exploring the membrane-disrupting intermediate states and key peptide-lipid interactions along the membrane-associated fibrillation pathways; (4) Exploring the membrane fragmentation mechanisms induced by beta-amyloid oligomers.

Cross-Seeded Fibrillation Between Post-Translationally Modified and Wild-Type Beta-Amyloid Variants and Structural Polymorphisms

The project studies the cross-seeded fibrillation processes between the wild-type beta-amyloid peptides and multiple types of post-translationally modified beta-amyloid fibril seeds. The modified beta-amyloid variants are present in the human pathological plaques, showing triggering effects to the amyloidosis of wild-type beta-amyloid peptides. We aim to answer the following fundamental questions: (1) What are the molecular structural differences in the fibrils formed by N-terminal post-translationally modified beta-amyloid peptides? (2) How would the N-terminal modifications on beta-amyloid peptides trigger the pathologically relevant consequences of wild-type beta-amyloid fibrillation? (3) Will structural polymorphisms induced by N-terminal modifications of beta-amyloid peptides propagate in cellular systems?

Membrane Interactions of the Drug-Delivery pH-Low Insertion Peptides

This collaborative project studies the molecular mechanisms of pH-dependent membrane interactions of the pH-Low Insertion Peptide, which is a peptide used for anti-cancer drug delivery. We specifically probe the intermediate states induced by the protonation of charged residues along the peptide sequences. These intermediate states define the process of membrane insertion as the microenvironmental pH drops from the physiological value down to the pH around cancerous cells.

bottom of page