Professor Jong-in Hahm of the Department of Chemistry at Georgetown University is supported by the Macromolecular, Supramolecular, and Nanochemistry (MSN) Program of the Division of Chemistry to study protein adsorption on surfaces. The study is focused on how proteins adhere and accumulate on the surfaces of nano-patterned polymeric materials. Protein adsorption on polymer surfaces impacts numerous everyday applications such as food packaging, health devices (contact lenses, artificial joints and implanted stents), diagnostic tools, and biosensors. The objectives of this research is to obtain a molecular-level understanding of the complex mechanisms underlying protein adsorption and to identify protein behavior on polymeric surfaces at the nanoscale level. The knowledge obtained from this research may aid in the development of protein assemblies for miniaturized and function-tailored biomaterials, biodevices, and tissue engineering scaffolds. Educational and outreach activities are integrated with the research activities. These include harnessing diversity through participation of underrepresented groups of undergraduate and high school students; enhancing student learning experiences through a newly-developed course in soft matter characterization; and promoting student networking opportunities in extended scientific exchange settings beyond Georgetown University.
The project aims are to elucidate noncompetitive and competitive protein adsorption characteristics at the individual biomolecular level on block copolymer (BCP) nanodomain surfaces that are precisely tuned for BCP's chemical composition, periodicity, and alignment. The research also seeks to determine the effects of the BCP nanodomain-related variables on the adsorption characteristics for a broad range of useful model proteins and to establish a highly effective method for rapidly and precisely creating nanoscale-patterned proteins with their orientation and alignment controlled over large substrate areas. By revealing important nanoscale protein adsorption characteristics of single and multi-protein systems that are unanswered to date, the study may provide much needed, direct experimental data for nanoscale protein adsorption with spatial resolution at or below the individual protein level and at each BCP nanodomain level. New fundamental toolsets are anticipated from the study in terms of tuning the physical and chemical parameters of BCP surfaces to effectively guide and control the large-area organization of given proteins.
This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.
