Currently Pete is working as a postdoctoral researcher at Chulalongkorn University Systems Biology center (CUSB), since April 2016. At CUSB, he implemented multiple bottom-up proteomics technologies to unveil functions, mechanisms, interacting proteins, post-translational modifications in signaling pathway involved in immunology. Especially our goal is to learn more about autoimmune disease, such as Systemic Lupus Erythematosus or SLE. At CUSB center we utilized home-made polyclonal antibodies to perform immunoprecipitation to study interacting proteins and coupled to mass spectrometry, so called affinity purification mass spectrometry (AP-MS). He aims to contribute his knowledge and expertise in mass spectrometry analysis to the research center. To learn more about our research, please visit CUSB website.
His previous doctoral researches were conducted in Professor Joseph Loo’s laboratory. He specializes in studying intact protein, protein-ligand interactions, and protein complexes by top-down mass spectrometry with native electrospray ionization (ESI). With the top-down approach, intact proteins are fragmented into small pieces. He utilized fragmentation techniques called electron capture dissociation (ECD). ECD can specially fragment protein backbone without disrupting weak intereactions. Thus, ligands, drugs, or anything that binds to the protein is still attached to fragments. By measuring an accurate mass of these ligand-bound fragments with high resolution Fourier transform ion cyclotron mass spectrometer (FT-ICR MS), he can characterize binding affinity, locate the binding site, and obtain some structural information of the protein complexes, in a single analysis. It is more like solving jigsaw puzzles. One of his project focuses on a synthetic compound called CLR01 that targets to some proteins that form amyloid and cause neurodegenerative disorders, such as Alzheimer’s and Parkinson’s diseases. The CLR01 compound has been shown to dissociate amyloid fibrils and become a potential drug candidate to cure the disease. By the top-down approach, he successfully revealed the binding site and its affinity on alpha-synuclein, which causes Parkinson’s disease. The observation is a key to understand how the compound works. He is also interested in applying some external ion activation (i.e. collisional, and vibrational, and photon energies) and chemical additives (supercharging agents) to enhance the protein fragmentation efficiency.
The most updated publication list can be found at Google Scholar