INSPIRE Faculty:

 
Dr. Priyanka Bajaj

Phone:

 
6665496

Contact Address

 
Room No., 202, GN Ramachandran Protein Center.

Write-up of research and development interests/focus, past and present goals:


Expertise:

Protein Engineering and Evolution, Biocatalysis


R & D interests:

My group’s main area of research focus is engineering and evolution of pharmaceutically important proteins. Currently, proteins are in high demand by pharmaceutical industry as Biotherapeutics and Biocatalyst and are a multibillion dollar industry. However, Most of these proteins in development for use as biotherapeutic and biocatalyst have challenges like low expression in various cell lines, issues with protein misfolding difficult downstream processing, low stability, immunogenicity and others. My research work is to resolve the above issues by using protein engineering and evolution tools and successfully develop these molecules for use in biotherapeutics an biocatalysis.

Selected list of Publications and Patents:

  • Moore E.J., Steck V., Bajaj, Pand Fasan, R (2017)Chemoselective Cyclopropanation over Carbene Y-H insertion Catalyzed by an Engineered Carbene Transferase. J. Org. Chem.,83(14):7480-7490. (IF=6)
  • Bajaj P., Sreenilayam, G., Tyagi, V., and Fasan, R. (2016)Gram-Scale Synthesis of Chiral Cyclopropane- Containing Drugs and Drug Precursors with Engineered Myoglobin Catalysts Featuring Complementary Stereoselectivity. Angew. Chem.  Int. Ed.  Engl.55(52):16110-16114. (IF=12) 
  • Tyagi, V., Sreenilayam, G., Bajaj, P., Tinoco, A., and Fasan, R. (2016) Biocatalytic Synthesis of Allylic and Allenyl Sulfides through a Myoglobin-Catalyzed Doyle-Kirmse Reaction.Angew. Chem. Int. Ed. Engl. 55(43):13562-13566. (IF=12) 
  • Bajaj P., Aggarwal, G., Tripathy, R.K. and Pande, A.H. (2014) Interplay between amino acid residues at positions 192 and 115 in modulating hydrolytic activities of human paraoxonase 1. Biochimie. 105, 202-210. 
  • Bajaj P., Tripathy, R.K., Aggarwal, G. and Pande, A.H. (2013). Characterization of human paraoxonase 1 variants suggests that his residues at 115 and 134 positions are not always needed for the lactonase/arylesterase activities of the enzyme. Protein Sci. 22, 1799-1807.

Present group members:

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