RECCR Rensselaer Exploratory Center for Cheminformatics Research




Homology Modeling


Co-PI: Steven Cramer

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Co-Investigator: Steven Cramer

Professor, Department of Chemical and Biological Engineering Rensselaer Polytechnic Institute

The development of efficient bioseparation processes for the production of high-purity biopharmaceuticals is one of the most pressing challenges facing the pharmaceutical and biotechnology industries today. In addition, high-resolution separations for proteomic applications are becoming increasingly important. Developing elution or displacement methodologies to remove closely related impurities often requires a significant amount of experimentation to find the proper combination of stationary phase material, salt type, pH, gradient conditions and/or displacers to achieve sufficient selectivity and productivity in these separation techniques.

Ion-exchange chromatography is perhaps the most widely employed chromatographic mode in the downstream processing of biomolecules. Generally, ion-exchange chromatography is regarded as occurring due to charge-based interactions between the solute, mobile phase components, and the ligands on the stationary phase. However, in addition to electrostatics, non-specific interactions have also been shown to effect separations in ion-exchange systems (Rahman et al. 1990; Law et al. 1993; Shukla et al. 1998b) . Hydrophobic interaction chromatography (HIC) is another technique that is commonly employed in the biotech industry due to the mild conditions employed relative to the harsh, denaturing conditions used in RPLC. However, almost all QSPR work in HPLC has focused on the adsorption of small molecules in reversed-phase systems. Our group has been instrumental in the developme