Jeffery A. Lowell, M.D. champions organ donation awareness		Search View past issues

Welfare use more common than many think Many Americans believe that welfare use happens to someone else, to people outside of mainstream society. But a study published in a recent issue of Social Work casts considerable doubt on that notion, finding that nearly two-thirds of all Americans between 20 and 65 will at some point turn to a public assistance program. Full story More Stories
				Researcher seeks ways to prevent protein misfolding By Tony Fitzpatrick A University biomedical engineer is unlocking the rules Mother Nature abides by in knowing "when to hold 'em or fold 'em." Photo by Bob Boston Rohit Pappu, Ph.D. (left), assistant professor of biomedical engineering, discusses a protein model with students Rachel Nordgren and Patrick Alford. Pappu's studies of protein misfolding could provide new information regarding the onset of numerous diseases, including Alzheimer's and Parkinson's. He's not dealing with cards; rather, with proteins -- products that carry out the plans of our genes. The biological function of proteins is directly determined by their folded shape in three-dimensions. The folding process is a thermodynamically driven reaction modulated by changes in environmental parameters such as temperature, solvent conditions, protein concentration as well as by mutations in amino acid (the building blocks of proteins) sequence. Rohit Pappu, Ph.D., assistant professor of biomedical engineering, is developing computational models for understanding the formation of misfolded proteins and amyloid fibrils, bundled substances that are associated with several diseases. Changes in any of these parameters can lead to errors in the folding process. These misfolded proteins lead to irreversible protein aggregation and subsequent disease. Protein misfolding is associated with the onset of Alzheimer's disease, bovine spongiform encephelopathy or "mad cow disease," Cruetzfeldt-Jakob disease, cystic fibrosis, emphysema, Huntington's disease, Parkinson's disease, type II diabetes and some types of spinocerebellar ataxia, as well as several other diseases. These diseases, referred to as amyloidoses, are characterized by the deposition of insoluble protein aggregates or amyloid fibrils resulting from misfolded proteins. This misfolding leads to irreversible protein aggregation. A vast number of amino acid sequences of disparate lengths form amyloid fibrils. "Clearly there are universal principles that underlie the misfolding process," Pappu said. "I am using simple peptide systems with well-defined folded states to understand these universal physical principles." His recent work on the organizing principles for structure in unfolded peptides will serve as bedrock for further research in the misfolding of single chains of polypeptides as well as interactions among many chains.

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