[CCoE Notice] PhD Defense Announcement

[Khator, Suresh]

Ph.D. Defense Announcement
Wen-Hsiang Chen, Friday, July 15, 2011, 10:00 AM
Mechanical Engineering Large Conference Room (#202)
Major Professor: Dr. Richard Willson

Biomolecule Adsorption: Materials and Fundamentals

Proteins and nucleic acids are the essential biopolymers of living organisms. Manufactured nucleic acids and proteins are increasingly important therapeutics, e.g., insulin, antibodies in gene therapy and enzyme therapy to treat various diseases.  With the increasing need for these two types of biopolymers, rapid separations with high selectivity and specificity are in high demand. In this work, we will mainly discuss how we used the novelty of clustered-charge ion-exchange ligands to purify nucleic acids and proteins and how we characterized the clustered charge ion-exchange adsorbents at both ensemble and single-molecule levels.
At the ensemble level, the binding affinity and binding capacity of our clustered-charge penta-argininamide ion-exchange adsorbent and other conventional adsorbents were described by Langmuir isotherm and the DNA/RNA selectivity over various salt concentrations was measured and characterized by single-point adsorption isotherms. We observed that the clustered-charge penta-argininamide adsorbent showed higher binding affinity, capacity and selectivity compared to most of the conventional adsorbents even when the ligand density of our clustered-charge adsorbent was 10- to 100-fold lower than the density of the conventional ones. At the single-molecule level, the results showed that the adsorption of the dye-labeled protein of interest (*-Lactalbumin) could be monitored with confocal laser fluorescence microscopy. The diffusion coefficients of the dye-labeled protein on various surfaces, which were determined by fluorescence correlation spectroscopy (FCS), also suggested that we could detect the adsorption of single protein molecules on the clustered-charge peptide immobilized surface.
Finally, in an effort to extend the idea of clustered ligands to other types of adsorbents, we explored the preparation of clustered immobilized metal-ion affinity chromatography ligands by carboxymethylation of the primary amines on proteins and peptides.
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