The Organic and Macromolecular Chemistry Program in the Chemistry Division at the National Science Foundation supports Professor Laurence S. Romsted at Rutgers University in New Brunswick NJ. He proposes to do three projects that combine the logic of pseudophase models with the power of his arenediazonium probe method. These projects will determine the concentrations of weakly basic nucleophiles, including water, in the interfacial regions of surfactant based association colloids, and rate constants for reactions with antioxidants in opaque emulsions. The results should give new insight into the contribution of ion-pairing and hydration to the balance of forces controlling aggregate morphology; new information on the conformations and orientations of polypeptides at membrane mimetic surfaces; and a new understanding of previously unattainable determinations of antioxidant reactivity and distribution in emulsions. Completion of the projects will deepen current understanding of the balance of forces controlling surfactant aggregate structure. They will aid in refining the 'tuning' of the structures of soft materials and enhance their utility as encapsulating agents, thickeners, and fluids for bulk transport. The conformation and orientation of the HIV-1 surface glycoprotein, gp41, which is important in the cell fusion mechanism leading to AIDS, will be viewed at interfaces from a new chemical perspective. The creation of a scale of antioxidant efficiency will be of general utility and enhance both nutrition and health.In a broader sense, Professor Romsted's research program includes: (a) advanced training for undergraduate and graduate students and postdoctoral fellows; (b) scientific collaborations, including student and faculty exchanges, with colleagues in the US, France, Sweden, and Brazil; (c) continued participation in national and international meetings and publication in international journals; (d) strengthening the teaching of a graduate course in 'Supramolecules and Assemblies' and undergraduate organic chemistry; and (e) laying the conceptual basis for soft materials technologies. Thus, providing new insight into morphologies of membrane bound proteins, and improving safety and shelf-life of emulsified foods.
|Effective start/end date||5/1/09 → 4/30/12|
- National Science Foundation (National Science Foundation (NSF))
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