Friday, February 1, 2019
How to Treat Prion Diseases Essay -- Medical Disease
How to Treat Prion DiseasesAbstractScientists atomic number 18 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 century% 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 forthcoming today because drawbacks constantly prevent the development of efficient therapy. Studies continue to tardily progress, hoping to find methods to immunize against more prion diseases.ProblemNo one this instant has a solid understanding as to why TSE, or prion diseases, occur. The unreserved explanation is that PrP(c), the normal isoform of the prion protei n, is forced to fold into PrPSc, the other pathological isoform, causation the misfolded PrP(c) to acquire proteolytic enzyme-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 impertinently 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 piling proteins or peptides, deeming the protease-sensitive proteins soluble so during ... ...r to the fatal TSE.8b10ReferencesBainbridge, J., Jones, N., & Walker, B. (2004, May 12). bigeminal antigenic peptides facilitate generation of anti-prion antibodies. Retrieved July 26, 2008, from http//www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1809119Graham, S. (2002, July 30). Common Antibiotic Saps Prions Strength. Retrieved July 24, 2008, from http//www.sciam.com/article.cfm?id=common-antibiotic-saps-prKorth, C., Streit, P., & Oesch, B. (1999). Monoclonal Antibodies limited 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 target New Promise in Combating Prion Diseases. Retrieved July 24, 2008, from http//www.sciam.com/article.cfm?id=old-drugs-show-new-promis
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