How to Treat Prion Diseases Essay -- Medical Disease

How to Treat Prion Diseases Abstract Scientists are stumped as to the development and nature of proteinaceous infectious particles. Neither virus nor bacteria, these prions, are believed to cause transmissible spongiform encephalopathies (TSE), rare diseases said to be 100% fatal, without possessing nucleic acids. Their unhindered growth is thought to be the cause for bovine spongiform encephalopathy (BSE), or Mad Cow Disease, Creutzfeldt-Jakob (CJD), scrapie and other TSE, diseases characterized by the brain microscopically turning into sponge-like matter. There are no cures or effective treatments available today because drawbacks constantly prevent the development of efficient therapy. Studies continue to slowly progress, hoping to find methods to immunize against more prion diseases. Problem No one presently has a solid understanding as to why TSE, or prion diseases, occur. The simple explanation is that PrP(c), the normal isoform of the prion protein, is forced to fold into PrPSc, the other pathological isoform, causing the misfolded PrP(c) to acquire protease-resistance. As to a physical presentation, a clumped protein consisting primarily of alpha-helices (spirals) is converted into one consisting primarily of beta-sheets (sets of pleated hairpins). In an essence, alpha-helical content decreases while beta-sheet content increases. The newly converted protein then possesses the same characteristics as those of the native PrPSc (Korth, Streit, & Oesch, 1999). PrPSc acquires partial protease resistance upon the transformation and passes this resistance along to the naturally protease-sensitive PrP(c). Protease is an enzyme that breaks down proteins or peptides, deeming the protease-sensitive proteins soluble; so during ... ...r to the fatal TSE. 8 b10 References Bainbridge, J., Jones, N., & Walker, B. (2004, May 12). Multiple antigenic peptides facilitate generation of anti-prion antibodies. Retrieved July 26, 2008, from http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1809119# Graham, S. (2002, July 30). Common Antibiotic Saps Prions' Strength. Retrieved July 24, 2008, from http://www.sciam.com/article.cfm?id=common-antibiotic-saps-pr Korth, C., Streit, P., & Oesch, B. (1999). Monoclonal Antibodies Specific for the Native, Disease-Associated Isoform of the Prion Protein. Methods in ENZYMOLOGY: , 309, 106-122 . Soto, C. (2006). Prions: The New Biology of Proteins. Taylor & Francis Group: CRC Press. Wong, K. (2001, August 14). Old Drugs Show New Promise in Combating Prion Diseases. Retrieved July 24, 2008, from http://www.sciam.com/article.cfm?id=old-drugs-show-new-promis