Join us for Research Recognition Day.

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Research Recognition Day is our signature annual event in celebration of research done by students, clinicians, and researchers. 

You have the opportunity to explore and evaluate research in clinical pharmacy, translational medicine, drug metabolism, pharmacokinetics, pharmacogenomics, proteomics, formulation development, medicinal chemistry, pharmacology, drug delivery, and more. 

Hear our 2024 Keynote Speaker Omar Galárraga, PhD, present "Economic-based Interventions and Policies to Improve Health Outcomes". Dr. Galárraga will draw from past and current research, including NIH-funded R01 projects, "Integrated Community-Based Care for HIV/NCD care and Microfinance in Kenya: A Clustered RCT", "Insurance-Based Monetary Incentives to Promote Regular Exercise: an RCT", and "Rigorous Non-Experimental Evaluation of Medicaid Policies affecting Persons Living with HIV in the US". He is the Director of the Health Services Research PhD Program at Brown University School of Public Health, has authored over 130 scientific papers, and serves as associate editor for "Health Economics". 

The Temple University School of Pharmacy gratefully acknowledges Title Sponsors Dan Castiglia and Soo Ham, Pharmacy Class of 1998. Dan, a loyal champion for research at Temple University, has long been a supporter of Research Recognition Day. Dan and Soo represent pharmacy careers in the pharmaceutical industry and community pharmacy, respectively, and are married with two children.


Poster 6

Determination of the potency of different inhibitors of blood esterases using an optimized 96 well plate-based assay.

Primary Student: Tashnuva Rifat

Faculty:  Dr. Marc Ilies


Different esterases present in blood hydrolyze a plethora of esters with different lipophilicity. Some have a preference for more hydrophilic substrates, while others prefer lipophilic substrates. We have shown that the activity of these esterase can be evaluated either by the hydrolysis of 4 nitrophenyl acetate (4NPA) for esterases preferring hydrophilic substrate (e.g. carbonic anhydrase) or 4 nitrophenyl palmitate (4NPP) for esterase preferring lipophilic substrate (e.g. classical lipase, lipoprotein lipase). Based on these reactions, we also developed a 96 well plate-based assay for carbonic anhydrase enzyme and classical lipase enzyme and we validated the assay by determining their kinetic parameters of these esterases. Using this optimized plate assay, we were able to assess the potency of different inhibitors against these two enzymes, both reversible and irreversible.


The assays involving the hydrolysis of 4NPA for bovine carbonic anhydrase (bCAII) and 4NPP for Lipase Pseudomonas cepacia (LPC) were developed in a 96 well plate format and the Vmax and Km values for both esterases were determined using classical Michaelis-Menten kinetics. Stock solution of different inhibitors of these enzymes were made in dmso and their potency was determined following serial dilutions of the dmso stock, using the above-mentioned assay.


The Vmax and km value for bCAII were 4.1 µM/min and 1.37mM and Vmax and km value for LPC were 7.04µM/min and 0.777mM respectively. The IC50 and Ki value of several CA and LPC values were determined and were found to be in good agreement with published values. Several known amphiphilic esterase inhibitors were assessed on LPC for the first time.


The potency of different inhibitors was successfully determined using our optimized 96 well plate based assay for both carbonic anhydrase and lipase blood esterases.