Tzyh-Chang Hwang, MD, PhD

Tzyh-Chang Hwang, MD, PhD

Medical Pharmacology and Physiology

Dalton Cardiovascular Research Center Investigator



University of Missouri researcher Dr. Tzyh-Chang Hwang has worked to understand and treat cystic fibrosis.

Cystic fibrosis (CF) is the second most common lethal genetic disease in the United States. One thousand new cases are diagnosed each year, usually in young children. There is no cure, but thanks to dedicated medical researchers, life expectancy for those living with the disease continues to increase.

Hwang is among these dedicated researchers. He focuses his research on a protein molecule in the body, called the CFTR channel, by which chloride moves in and out of cells. CF is caused by mutations that reduce activity in this channel. Hwang identified two amino acids in the CFTR protein that act as a gate, regulating the flow of chloride ions through this important transport protein.

Funded by leading scientific organizations including the Cystic Fibrosis Foundation and the National Institutes of Health, Hwang has made discoveries that shed light on the mechanisms of CF. His advancements could potentially provide information for new drug development and treatments. Dr. Tzyh-Chang Hwang is a professor emeritus of medical pharmacology and physiology in the School of Medicine.

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Academic Information

Dalton Cardiovascular Research Center Investigator


134 Research Park Dr.
Columbia, MO 65212
United States

P. 573-882-2181

Research Interests

  • Cystic fibrosis
  • Ion channel physiology

Areas of Expertise

  • Ion channel biophysics
  • Cystic Fibrosis
  • ABC transporters
  • Epithelial physiology

Education & Training

Post-Graduate School

1990, PhD, Johns Hopkins University


  • Xiaolong Gao., Yonghong Bai, and Tzyh-Chang Hwang. (2013). Cysteine scanning of CFTR’s first transmembrane segment reveals its plausible roles in gating and permeation. Biophys. J. 104:786-797.
  • Kang-Yang Jih, and Tzyh-Chang Hwang. (2013). Vx-770 potentiates CFTR function by promoting decoupling between the gating cycle and ATP hydrolysis cycle. Proc. Natl. Acad. Sci. USA. 110:4404-4409.
  • Wen-Ying Lin, Kang-Yang Jih, and Tzyh-Chang Hwang. (2014). A single amino acid substitution converts ATP into an inhibitory ligand. J. Gen. Physiol.144:311-320.
  • Han-I Jeh, Juinn-Tyng Yeh, and Tzyh-Chang Hwang. (2015). Modulation of CFTR gating by permeant ions. J. Gen. Physiol. 145:47-60.
  • Xiaolong Gao, and Tzyh-Chang Hwang. (2015). Localizing a gate in CFTR. Proc. Natl. Acad. Sci. USA. 112:2461-2466.
  • Jingyao Zhang, and Tzyh-Chang Hwang. (2015). The Fifth Transmembrane Segment of Cystic Fibrosis Transmembrane conductance Regulator Contributes to its Anion Permeation Pathway. Biochemistry 54:3839-50.
  • Ying-Chun Yu, Yoshiro Sohma, and Tzyh-Chang Hwang. (2016). On the mechanism of gating defects caused by the R117H mutation in cystic fibrosis transmembrane conductance regulator. J. Physiol. 594:3227-3244.
  • Xiaolong Gao, and Tzyh-Chang Hwang. (2016). Spatial positioning of pore-lining residues affirms an asymmetrical contribution of CFTR’s transmembrane segments to its anion permeation pathway. J. Gen. Physiol. 147:407-422.
  • Wen-Ying Lin, Yoshiro Sohma, and Tzyh-Chang Hwang. (2016). Synergistic potentiation of CFTR gating by two chemically distinct potentiators ivacaftor (VX-770) and NPPB. Mole. Pharm. 90:275-285.