Dr. Ajay Lajmi

• Position: Assistant Professor
• Department: Chemistry
• Office Location: Building 58C, Room 204
• alajmi@uwf.edu
• Campus: 850.857.6363

Biography

Dr. Ajay Lajmi completed his Ph.D. in Bio-Organic Chemistry from New York University followed by a Post-doctoral research fellowship at the University of Pittsburgh in DNA-binding proteins where he developed protein expression, chromatographic purification, MALDI-MS analytical methods and DNA binding assays for alanine mutants of a transcriptional activator protein.

Prior to joining the UWF Chemistry Department, he spent 15 years in industrial R&D pioneering the membrane chromatographic separation and purification methods for biologics such as gene therapy viral vectors, nucleic acids, recombinant proteins, and monoclonal antibodies. He served as an industry mentor for three years in an IUCRC-NSF program to guide graduate students in biochemical technology. 

His research group's current interests are in the synthesis of small molecules for substrate binding for studying hydrolases and redox enzymes. Dr. Ajay Lajmi's research interest includes developing methods to synthesize molecules for targeted biochemical functional properties with potential applications in biotechnology. A core focus of the research group involves mentoring students to build a strong foundation for a future independent research career at the interface of biochemical technology and materials chemistry. Other areas of research interest include investigating the role of metal ions in protein folding pathways that aims to provide drug targets for related diseases. 

Research

Non-covalent interactions play a major role in many biochemical processes. One of the main goals in our research group is to examine such interactions in order to develop synthetic structures with designed functional properties. Another aspect of our research involves investigating interactions between biological molecules and synthetic materials that affect their structure and properties in separations and purification. Lastly, we aim to develop predictive tools for molecular recognition and function by utilizing a shape-complementarity framework that is prevalent in many biochemical pathways.

Publications

Langdon, B. B.; Mirhossaini, R. B.; Mabry, J. N.; Sriram, I.; Lajmi, A.; Zhang, Y.; Rojas, O. J.; Schwartz, D. K. Single-Molecule Resolution of Protein Dynamics on Polymeric Membrane Surfaces: The Roles of Spatial and Population Heterogeneity. ACS Applied Materials & Interfaces 2015, 7 (6), 3607–3617.

Patents: