Priya R. Banerjee, PhD

Priya Banergee.

Assistant Professor

229 Fronczak Hall
(716) 645-3444
prbanerj@buffalo.edu

Website 

 

Education

  • BS, University of Calcutta, India – 2005
  • MS, West Bengal University of Technology, India – 2007
  • PhD, University at Albany, SUNY – 2011
  • Postdoctoral Fellowship, The Scripps Research Institute – 2012-2017

Research Area

Specialties

Single-molecule biophysics, Intrinsically disordered proteins, Phase transition in proteins and nucleic Acids, Biomolecular engineering

Research Interests

Our lab focuses on understanding the physical principles of (non) folding and phase behavior of Intrinsically Disordered Proteins (IDPs) using sensitive, high-resolution single-molecule techniques. IDPs account for a significant portion of eukaryotic proteome(30 ‒ 50%). Although they challenge the classical protein structure-function paradigm, it is well established now that the disordered proteome performs important organizational, regulatory, and signaling functions in cells. Furthermore, IDPs are commonly associated with a broad repertoire of human diseases including neurodegeneration and cancer.

IDPs typically display a high degree of conformational plasticity and substantial structural heterogeneity, which severely limits the application of conventional ensemble methods of structural biology to elucidate their properties. Due to this, single-molecule methodologies are critical to study these dynamic biological systems by watching one molecule at a time. In our laboratory, we develop and apply advanced single-molecule fluorescence spectroscopy tools, in combination with fluorescence microscopy, complementary biophysical spectroscopy, and physical modeling. Additionally, we employ a diverse array of chemical and biological methods to interrogate our system of interest. Using this multidisciplinary strategy, we seek answers for how the specific amino acid sequence of IDPs control their individual interaction space in a multi-component system leading to (a) IDP coupled binding-folding behavior that encodes multi-functionality, and (b) IDP self-assembly into biomolecular condensates with tunable material properties. These answers will be critical in deciphering the molecular functions of the disordered proteome and mapping their operational pathways. By understanding IDP molecular properties, we can further explore plausible strategies for (i)ameliorating cellular homeostasis in disease states, and (ii) expanding the scope of bioinspired functional materials.

Awards and Honors

  • NIH Outstanding Investigator Award (2020)
  • Featured in JACS Young Investigator Issue (2020)
  • American Heart Association (AHA) postdoctoral fellowship (2015)
  • Distinguished Doctoral Dissertation Award (2012)

 

Selected Publications

For a complete list of publications, please see Google Scholar.

  • Sequence-encoded and Composition-dependent Protein-RNA Interactions Control Multiphasic Condensate Topologies. Kaur, T., Raju, M., Alshareedah, I., Davis, B. D., Potoyan, A. D., Banerjee, P. R.* 2021. Nature communications. DOI: https://doi.org/10.1038/s41467-021-21089-4
  • Quantifying Viscosity and Surface Tension of Multi-Component Protein-Nucleic Acid Condensates. Alshareedah, I., Thurston, G. M. & Banerjee, P. R.* 2021. Biophysical Journal. DOI: https://doi.org/10.1016/j.bpj.2021.01.005
  • Phase Transition of RNA-protein Complexes into Ordered Hollow Condensates. Alshareedah, I. Moosa, M. M., Raju, M., Potoyan, A. D., Banerjee, P. R.* 2020. Proc. Natl. Acad. Sci. (U.S.A). 117 (27) 15650-15658. DOI: https://doi.org/10.1073/pnas.1922365117
  • Methods for Characterizing the Material Properties of Biomolecular Condensates. Alshareedah, I., Kaur, T., Banerjee, P. R.* 2020. Methods in Enzymology; DOI: https://doi.org/10.1016/bs.mie.2020.06.009/
  • Molecular Crowding Tunes Material States of Ribonucleoprotein Condensates. Kaur, T., Alshareedah, I., Wang, W., Ngo, J., Moosa, M. M., Banerjee, P. R.* 2019. Biomolecules, 9(2), 71; DOI: https://doi.org/10.3390/biom9020071
  • Interplay Between Short-range Attraction and Long-range Repulsion Controls Reentrant Liquid Condensation of Ribonucleoprotein-RNA Complexes. Alshareedah, I., Kaur, T., Ngo, J., Seppala, H., Djomnang Kounatse, L.-A., Wang, W., Moosa, M. M., Banerjee, P. R.*, 2019. J. Am. Chem. Soc. 141, 37, 14593-14602. DOI: https://doi.org/10.1021/jacs.9b03689
  • Divalent Cations Can Control a   Switch-like   Behavior   in   Heterotypic    and    Homotypic    RNA    coacervates. Onuchic, P. L., Milin, A. N., Alshareedah, A., Deniz, A. A., Banerjee, P. R.* 2019. Scientific Reports, Vol 9, Article number: 12161. DOI: https://doi.org/10.1038/s41598-019-48457-x.
  • Reentrant Phase Transition Drives Dynamic Substructure Formation in Ribonucleoprotein Droplets. Banerjee, P. R.*, Milin, A. N., Moosa M. M., Onuchic, P. L., Deniz, A. A.* 2017. Angew Chem Int Ed Engl. 56(38):11354-11359. DOI: https://doi.org/10.1002/anie.201703191