Wen-Ji Dong, Ph.D.

Wen-Ji Dong, Ph.D.


Associate Professor (Bioengineering)
E-Mail: wdong@vetmed.wsu.edu
Office: Veterinary and Biomedical Research Building (VBR) room 271 
Phone:(509)335-5798



Current Positions

2010-Present Associate Professor Voiland School of Chem Eng WSU - Pullman, WA
2010-Present Associate Professor IPN, College of Vet Med WSU - Pullman, WA


Education

1992 Ph.D. Physical Chemistry, University of London (London France)
1985 Masters Coordinate Chemistry, Lanzhou University (P.R. China)
1982 B.S. Chemistry, Lanzhou University (P.R. China)


Prior Academic Appointments

1994-1996 Associate Research Fellow, Muscular Dystrophy
1996-2002 Research Instructor, University of Alabama - Birmingham, AL
2002-2005 Research Assistant Professor, University of Alabama - Birmingham, AL
2006-2010 Assistant Professor, WSU - Pullman, WA


Research

Research in my lab is multi-disciplinary. The primary objective of our research is to understand the Ca2+ switching mechanism of cardiac myofilament in healthy and diseased hearts. Cardiac muscle contraction is initiated by Ca2+ binding to cardiac troponin C triggering a series of functional structural changes within the thin filament. These serious structural transitions are regulated by both Ca2+ binding and cross-bridge cycling, and modulated by protein phosphorylation and cardiomyopathy mutations. A full understanding of these mechanisms is critical for research efforts to prevent, diagnose, and treat myocardial diseases. In our research we use various fluorescence spectroscopic approaches, including FRET, to acquire detailed functional, structural, thermodynamic, and kinetic knowledge associated with those thin filament structural transitions at the level of single regulatory unit, the fully reconstituted thin filament preparations and the chemically skinned muscle fibers. These studies will provide insights into mechanistic alterations of cardiac regulation in diseased heart, which may ultimately lead to design a fluorescence assay to screen drug candidates of Ca2+ sensitizer, a promising therapeutic drug for treatment of heart failure.

The second objective of our research is to design and develop various sensors for biological and cellular research and future clinical applications. One example is to develop an ultra-sensitive assay to establish PKA-phosphorylated cTnI (p-cTnI) in blood serum samples as potential cardiac biomarker for early heart disease detection. 

The third objective of our research is to develop novel luminescent materials and approaches for solar energy harvest applications, including wavelength-shifting materials and novel solar concentrators.


Current Funding

NIH/HLBI Kinetics of cardiac myofilament activation, PI


Publications

  1. Schlecht, W., et al., Fluorescence based characterization of calcium sensitizer action on the troponin complex. Chemical biology & drug design, 2016. 87(2): p. 171-181.
  2. Pulcastro, H.C., et al., Increased titin compliance reduced length-dependent contraction and slowed cross-bridge kinetics in skinned myocardial strips from Rbm20ΔRRM mice. Frontiers in Physiology, 2016. 7.
  3. Li, Y., et al., A structurally modified perylene dye for efficient luminescent solar concentrators. Solar Energy, 2016. 136: p. 668-674.
  4. Li, K.-L., et al., Sarcomere length dependent effects on the interaction between cTnC and cTnI in skinned papillary muscle strips. Archives of biochemistry and biophysics, 2016. 601: p. 69-79.
  5. Li, K.-L., et al., In situ time-resolved FRET reveals effects of sarcomere length on cardiac thin-filament activation. Biophysical journal, 2014. 107(3): p. 682-693.
  6. Jayasundar, J.J., et al., Molecular dynamics simulations of the cardiac troponin complex performed with FRET distances as restraints. PloS one, 2014. 9(2): p. e87135.
  7. Jacroux, T., et al., Cationic isotachophoresis separation of the biomarker cardiac troponin I from a high‐abundance contaminant, serum albumin. Electrophoresis, 2014. 35(14): p. 2029-2038.
  8. Zhou, Z., et al., Structural and kinetic effects of hypertrophic cardiomyopathy related mutations R146G/Q and R163W on the regulatory switching activity of rat cardiac troponin I. Archives of biochemistry and biophysics, 2013. 535(1): p. 56-67.
  9. Rieck, D.C., et al., Structural basis for the in situ Ca 2+ sensitization of cardiac troponin C by positive feedback from force-generating myosin cross-bridges. Archives of biochemistry and biophysics, 2013. 537(2): p. 198-209.
  10. Li, Y., et al., Increasing the power output of a CdTe solar cell via luminescent down shifting molecules with intramolecular charge transfer and aggregation-induced emission characteristics. Energy & Environmental Science, 2013. 6(10): p. 2907-2911.