Assistant Professor, Department of Biomedical Engineering, National University of Singapore
The scientific interest of our lab is at the interface of cell biology, biophysics, and advanced imaging technology. We are interested in developing and applying superresolution microscopy to study how proteins are assembled into nanoscale machinery within the cells, with current focus on the integrin-based adhesion complexes (focal adhesions).
The resolution of conventional fluorescence microscope is limited by diffraction to ~250 nm. The aim of super-resolution microscopy is to combine the exquisite sensitivity afforded by fluorescence with high spatial resolution in the nanometer scale, comparable to electron microscope.
We are interested in advancing methodologies and applications of superresolution microscopy through both optical instrumentation and computational approaches. We are building an iPALM instrument for 3-dimensional superresolution microscopy at the MBI and will use this platform for live cell imaging, and as an optical research platform. Some example iPALM images can be found here.
Integrin-mediated cell adhesions
Cell adhesion to the extracellular matrix (ECM) is mediated by integrin and numerous other signaling proteins. Integrin-based adhesions (commonly called Focal Adhesions) play essential roles in many cellular processes, such as migration, mechanotransduction, immune response. We have recently applied iPALM to decipher the molecular architecture of the Focal Adhesions, revealing for the first time a stratified organization that is spanned by talin. We plan to focus on the genesis of this architecture and the biophysical roles of the integrin receptors and large proteins during the assembly of the adhesions.
Nanoscale architecture of cellular structures
We have a broad interest in applying super-resolution microscopy to visualize the nanoscale architecture of subcellular structures. In addition to our ongoing interest is in the Focal Adhesions systems, we are open to collaboration to apply super-resolution techniques to other biological systems.
2007 Ph.D. (Biophysics) Stanford University
2001 A.B. Summa cum laude (Chemistry and Biological Sciences) Cornell University
P. Kanchanawong, G. Shtengel, A. Pasapera-Limon, E. Ramko, M.W. Davidson, H.F. Hess, C. M. Waterman. “Nanoscale Architecutre of Integrin-based Adhesions”, Nature, 468(7323): 580-4, 2010.
W.D. Shin, R.S. Fischer, P. Kanchanawong, Y. Kim, J. Lim, K.A. Meyers, Y. Nishimura, S.V. Plotnikov, I. Thievessen, D. Yarar, B. Sabass, C.M. Waterman, A Versatile, Multicolor Total Internal Reflection Fluorescence and Spinning Disk Confocal Microscope System for High-Resolution Live Cell Imaging, in: R.D. Goldman, J.R. Swedlow, D.L. Spector (Eds.), Live Cell Imaging: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 2010.
G. Shtengel, J. A. Galbraith, C. G. Galbraith, J. Lippincott-Schwartz, J. M. Gillette, S. Manley, R. Sougrat, C. M. Waterman, P. Kanchanawong, M. W. Davidson, R. D. Fetter and H. F. Hess. “Interferometric fluorescent super-resolution microscopy resolves 3D cellular ultrastructure”, Proc. Nat. Acad. Sci. USA, 106 (9), 3125-3130, 2009.
L. N. Silverman, P. Kanchanawong, T. P. Treynor, S. G. Boxer. “Stark spectroscopy of mixed valence systems”, Phil. Trans. R. Soc. A, 366, 33-45, 2008.
X. Shu, K. Kallio, X. Shi, P. Abbyad, P. Kanchanawong, W. Childs, S. G. Boxer, and S. J. Remington. “Ultrafast Excited-State Dynamics in the Green Fluorescent Protein Variant S65T/H148D. 1. Mutagenesis and Structural Studies”, Biochemistry, 46 (43), 12005 -12013, 2007.
X. Shi, Paul Abbyad, X. Shu, K. Kallio, P. Kanchanawong, W. Childs, S. J. Remington, and S. G. Boxer. “Ultrafast Excited-State Dynamics in the Green Fluorescent Protein Variant S65T/H148D. 2. Unusual Photophysical Properties”, Biochemistry, 46 (43), 12014 -12025, 2007.
P. Kanchanawong, M. G. Dahlbom, T. P. Treynor, J. R. Reimers, N.S. Hush and S. G. Boxer, “Charge delocalization in the special pair radical cation of mutant reaction centers of Rhodobacter sphaeroides from Stark spectra and non-adiabatic spectral simulations”, J. Phys. Chem. B. 110 (37), 18688-18702, 2006.
G. Andre, P. Kanchanawong, R. Palma, H. Cho, X. Deng, D. Irwin, M. E. Himmel, D. B. Wilson and J. W. Brady, “Computational and experimental studies of the catalytic mechanism of Thermobifida fusca Cellulase Cel6A (E2)”, Protein Engineering. Vol. 16: 125-134, 2003.