Chi-cheng received a BSc in chemistry from National Tsing Hua University in 2003. He then moved to the University of Texas at Dallas and obtained his MSc in chemistry in 2007 for his work on studying proteins interacting with carbon nanotubes using molecular simulations under the supervision of Professor Steven O. Nielsen. He received his PhD in 2010 working on characterizing the interfacial energy at the nanoscale and the self-assembly of carbon based nanoparticles with biological membranes.
In 2010, he joined Professor Juan de Pablo’s group as a postdoctoral research at the University of Wisconsin-Madison, and studied the misfolding of amyloid peptides. He then moved with the lab to the Pritzker School of Molecular Engineering at the University of Chicago and the Material Science Division at Argonne National Lab. Currently he is investigating the self-assembly and aggregation of amyloid peptides using multiscale molecular simulation. His research interests include the design, self-assembly, and application of soft condensed materials including proteins, lipids, nucleotides, and copolymers.
Amyloid fibrils are highly ordered, β-sheet rich protein aggregates. They are best known for their associations with various diseases, including Alzheimer’s disease, Parkinson’s disease, and type II diabetes. On the other hand, natural occurring amyloid fibrils, including spider silks and curli fibrils, hold positive biological functions. These non-pathological amyloid fibrils exhibit unique physical and mechanical properties with great potential in bionanomaterials. Understanding the mechanism of peptide self-assembly into fibrils is critical to control the structures and functions of amyloid materials as well as develop therapeutic strategies for pathological amyloids.
Chi-cheng's research currently focuses on the pathological amyloid proteins including human amylin (type II diabetes), poly-glutamine (Huntington’s disease), and amyloid-β (Alzheimer’s disease). He uses multiscale molecular simulations with a variety of enhanced sampling techniques, including bias-exchange metadynamics, transition path sampling, and forward flux sampling, to study monomer structures and the conformational transitions of amyloid forming peptides. He also investigates the protein aggregation pathways and the associated kinetics and free energy landscapes in different environments, including water, aqueous trehalose, and biological membranes.
Fibrillar dimer formation of islet amyloid polypeptides
Chiu, Chi-cheng, and Juan J. De Pablo. "Fibrillar dimer formation of islet amyloid polypeptides." AIP Advances 5.9 (2015): 092501.
Secondary structure of rat and human amylin across force fields
Hoffmann, Kyle Quynn, et al. "Secondary structure of rat and human amylin across force fields." PloS one 10.7 (2015): e0134091.
Basis Function Sampling: A New Paradigm for Material Property Computation
J. K. Whitmer, C. Chiu, A. A. Joshi, and J. J. de Pablo. Basis Function Sampling. PRL. 2014. Vol. 113, Pg. 190602.
Effect of Proline Mutations on the Monomer Conformations of Amylin
Chiu, Chi-cheng; Singh, Sadanand and de Pablo, Juan J.. Effect of Proline Mutations on the Monomer Conformations of Amylin. Biophysical Journal. 2013. Vol. 105, Pg. 1227-1235.