个人简介

DARPA Young Faculty Award, 2011; NIH Director’s New Innovator Award, 2009; ACS PROGRESS/Dreyfus Lectureship, 2008; NIH Research Scholar Development Award, 2007; NIH Ruth L. Kirschstein Postdoctoral Fellowship, 2004-2006

研究领域

Chemical and Biological Imaging/Materials Chemistry/Molecular Biophysics/Nanoscience and Technology/Physical Chemistry

The goal of research in the Payne Lab is to understand the underlying molecular mechanisms by which cells interact with synthetic materials. Recent developments in a broad range of scientific disciplines including microscopy, spectroscopy, cell biology, materials science, and structural biology have created a unique opportunity to probe this question directly. Students in the Payne Lab draw upon these scientific disciplines for a highly interdisciplinary research experience. Nanoparticle-cell interactions. Nanoparticles have important biomedical applications ranging from the treatment of human disease with gene therapy to understanding basic cellular functions with fluorescent probes. In all of these applications, nanoparticles come into contact with a complex mixture of extracellular proteins. The Payne Lab is interested in understanding how adsorption of proteins onto the surface of a nanoparticle alters the interaction of the nanoparticle with a cell. By understanding how nanoparticles interact with cells in a realistic biological environment, we will be able to design better nanoparticles for the treatment and detection of human disease. Conducting polymer-cell interactions. The delivery of biocompatible conducting polymers into cells has important applications in regenerative medicine. The Payne Lab is using their expertise in nanoparticle delivery to develop methods for conducting polymer delivery. In addition, the Payne Lab is using cells and biomolecules as catalysts for the polymerization of conducting polymers with tunable properties. Fluorescence microscopy. Observing the interactions of cells with materials requires the spatial and temporal resolution provided by fluorescence microscopy. While recent developments in fluorescence microscopy make it possible to image many of the dynamic events that are essential to cellular function, new methods are necessary to observe the dynamics of single molecules inside living cells. Imaging within live cells is difficult as the emission from fluorescent probes competes with the autofluorescence of the cell. The Payne Lab is developing new optical techniques for quantitative cellular imaging. Optical methods of interest include nanometer-level imaging, spectroscopic single-particle tracking, and multiphoton total internal reflection microscopy.

近期论文

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“Hemoglobin-mediated synthesis of PEDOT:PSS: Enhancing conductivity through biological oxidants,” J.D. Morris, D. Khanal, J.A. Richey, C.K. Payne, Biomaterials Science, in press (2015). "Cellular binding of nanoparticles disrupts the membrane potential," E.A.K. Warren and C.K. Payne, RSC Advances, 5, 13660-13666 (2015). "PEGylated nanoparticles: Protein corona and secondary structure," Sabiha Runa, Alexandra Hill, Victoria L. Cochran, Christine K. Payne, Physical Chemistry of Nanomaterials and Interfaces XIII, Proceedings of SPIE, 91651F, 2014. "A model for controlling the resting membrane potential of cells using nanoparticles." S. Mukhopadhyay, F. Zhang, E. Warren and C.K. Payne, IEEE Conference on Decision and Control, 2014. "Impact of serum proteins on MRI contrast agents: Cellular binding and T2 relaxation," A. Hill and C.K. Payne, RSC Advances, 4, 31735-31744 (2014). "Nanoparticle-cell interactions: Molecular structure of the protein corona and cellular outcomes," C.C. Fleischer and C.K. Payne, Acc. Chem. Res., 47, 2651-2659 (2014). "Secondary structure of corona proteins determines the cell surface receptors used by nanoparticles," C.C. Fleischer and C.K. Payne, J. Phys. Chem. B., Special Issue: Spectroscopy of Nano- and Biomaterials Symposium, 118, 14017-14026 (2014). Link "Tuning PEDOT:PSS conductivity with iron oxidants," J.D. Morris and C.K. Payne, Organic Electronics, 15, 1707-1710 (2014). Link "Lysosome transport as a function of lysosome diameter," D. Bandyopadhyay, A. Cyphersmith, J.A. Zapata, Y.J. Kim, and C.K. Payne, PLoS One, 9, e86847 (2014). Link "Cellular binding of anionic nanoparticles is inhibited by serum proteins independent of nanoparticle composition," C.C. Fleischer, U. Kumar, and C.K. Payne, Biomaterials Science, 1, 975-982 (2013). "Protein-mediated synthesis of the conducting polymer PEDOT:PSS," S.M. Hira and C.K. Payne, Synthetic Metals, 176, 104-107 (2013). "Membrane potential mediates the cellular binding of nanoparticles," E.H. Shin, Y. Li, U. Kumar, H.V. Sureka, X. Zhang, and C.K. Payne, Nanoscale, 5, 5879-5886 (2013). Link "Conditioned media downregulates nuclear expression of Nrf2," S. Sarkar, C.K. Payne, and M.L. Kemp, Cellular and Molecular Bioengineering, 6, 130-137 (2013). "Imaging intracellular quantum dots: Fluorescence microscopy and transmission electron microscopy," C.J. Szymanski, H. Yi, J.L. Liu, E.R. Wright, C.K. Payne, Nanobiotechnology Protocols, Eds. S.J. Rosenthal and D.W. Wright (Humana Press, New York, 2013). "Nanoparticle surface charge mediates the cellular receptors used by protein-nanoparticle complexes," C.C. Fleischer and C.K. Payne, J. Phys. Chem. B, 116, 8901-8907 (2012). "Imaging lysosomal enzyme activity in live cells using self-quenched substrates," W.H. Humphries and C.K. Payne, Analytical Biochemistry, 424, 178-183 (2012). "Fluorescent coumarin thiols measure biological redox couples," K.G. Reddie, W.H. Humphries, C.P. Bain, C.K. Payne, M.L. Kemp, and N. Murthy, Organic Letters, 14, 680-683 (2012). "Nanoparticles act as protein carriers during cellular internalization," G.W. Doorley and C.K. Payne, Chem. Commun., 48, 2961-2963 (2012). "Endo-lysosomal vesicles positive for Rab7 and LAMP1 are terminal vesicles for the transport of dextran," W.H. Humphries IV, C.J. Szymanski, and C.K. Payne, PLoS ONE 6, e26626 (2011). doi:10.1371/journal.pone.0026626. Link "Single particle tracking as a method to resolve differences in highly colocalized proteins," C.J. Szymanski, W.H. Humphries IV, C.K. Payne, Analyst, 136, 3527-3533 (2011).