Chemistry, Department of


First Advisor

David S. Hage

Date of this Version



Suh, K., Sharmeen, S., Hage, D. (2020) Analysis of Hydroxychloroquine Interaction with Serum Proteins by High Performance Affinity Chromatography. Poster presentation, Spring Research Fair, University of Nebraska-Lincoln


Copyright 2020 by the authors


Personalized medicine or precision medicine has been an emerging market for better treatments of patients under varying physiological conditions.To improve the development of personalized medicine, a higher understanding of drug-protein binding between serum transport proteins and the unbound form of pharmaceuticals is needed. Human Serum Albumin (HSA) and Alpha1-acidglycoprotein (AGP) play a crucial role in pharmacokinetics as they are two most abundant transport serum proteins in body circulatory system. Inter-individual variabilities of serum proteins, such as the physiological condition of patients, have been believed to alter the drug-serum protein binding. Fig. 1 shows an example of the cause of inter-individual variabilities of AGP by various degree of glycans.

This study examined the interaction between hydroxychloroquine and serum proteins, HAS and AGP. AGP fractions with bi-antennary glycans and tri-tetra-antennary were separated by lectin affinity chromatography using ConcanavalinA and were used for affinity microcolumns. Entrapment of serum proteins can result in the use of intact serum proteins. Zonal elution results indicated the different contribution of the different glycoforms of AGP onto hydroxychloroquine binding. Ultrafast affinity extraction provided a relatively fast and precise binding information of hydroxychloroquine to serum proteins. The information obtained by this study can provide a better understanding for estimating hydroxychloroquine-serum protein interactions.