SUMMER RESEARCH TRAINING IN MEMBRANE SCIENCE AND TECHNOLOGY 2008 NSF REU SITE PROGRAM at the UNIVERSITY OF CINCINNATI
The Department of Chemical & Materials Engineering, College of Engineering is pleased to offer this research project as part of  the 2007 summer NSF-REU Site Program administered by the Department of Pharmacology & Cell Biophysics.  Students interested in this project are urged to contact Professor Smirniotis to discover more about the project, learn what your responsibilities will be during the ten-week research training program.
Project #: 08 - 020  (NOT AVAILABLE for Summer 2008) Faculty Supervisor/Mentor: Panagiotis (Peter) Smirniotis, Ph.D., Professor Chemical & Materials Engineering College of Engineering Email: panagiotis.smirniotis@uc.edu
Nano-structured Membranes for Preparative Purifications of Biopharmaceuticals
General background and significance of the project: This REU project will integrate with an interdisciplinary program for the development and understanding of novel inorganic nanoporous functionalized membranes for the purification and/or separation of proteins and related biomolecules.  Proteins and monoclonal antibodies (MAbs) are of great importance in the evolving biopharmaceutical industry. The commercial production of these compounds as therapeutic drugs continues to be challenged by limitations in downstream purification techniques. Two issues of prime importance are the availability of highly selective adsorbents and membranes for the large variety of separations that are of commercial significance, and an incomplete understanding of the process of biomolecular adsorption/desorption. Selected mesoporous materials, namely SBA-15 (1-dimensional) and to a less extent SBA-11 (3-dimensional), will be investigated. Based on our experience, synthesis techniques will be developed to make materials for membrane chromatography in preparative bioseparations.  The pores of these membranes will be functionalized to promote specific interactions with targeted biomolecules. The modified membranes will be studied for overloaded (high capacity) chromatographic purifications. The proposed materials are expected to demonstrate unique features that will enable high throughput operations, high selectivities, and the ability to tailor physical and chemical properties of the membranes (hydrophobicity/hydrophilicity, surface area, pore size, etc.) to provide a new level of versatility for bioseparations.
Brief description of proposed research and activities for the 10-week REU period: This REU project research will provide valuable new data on the interactions of proteins with solid surfaces. The focus of the proposed work will be on ion-exchange membranes, because of its recognized importance in aqueous-based purifications of proteins and Monoclonal Antibodies (MAbs). Using established experimental characterization techniques, the influences of surface functionality, protein characteristics and solution composition on equilibrium capacity and rates of adsorption will be studied. In particular, behavior under non-linear (overloaded) conditions is of interest, since this is of importance for process-scale bio-separations. Fundamental insights obtained from the data are expected to contribute to an improved understanding of the adsorption of proteins, and, consequently, the development of improved models for the design and optimization of process-scale systems.
What the REU Student can gain from participating in this project: The REU student will synthesize membranes, SBA-11 (cubic), which crystallizes at relatively high template concentration, will be deposited on the substrate in a controlled manner to ensure satisfactory fluxes. The REU student will perform adsorption/desorption isotherm measurements, rate of adsorption/desorption studies, chromatography, microcalorimetry, and zeta potential measurements to elucidate the mechanisms of retention. Significant contributions by the REU student will be included with co-authorship in meeting presentations and peer-reviewed articles arising from this research.