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Prion Protein Aggregation and FibrillogenesisIn Vitro

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Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease

Part of the book series: Subcellular Biochemistry ((SCBI,volume 65))

Abstract

This chapter focuses on the structural conversion of natural and recombinant prion proteins in vitro. They key event in prion diseases is the conversion of the cellular prion protein (PrPC) into its disease causing isoform PrPSc. This conversion is represented by a conformational change from an β-helical dominated isoform into the mostly β-sheeted PrPSc. Represented is an overview of in vitro conversion systems that result in β-structured recombinant prion proteins including the current achievements in the generation of synthetic mammalian prions as proof of the protein-only hypothesis. In addition to the conversion of recombinant PrP the chapter features a summary of the protein misfolding cyclic amplification (PMCA) technique which has gained enormous popularity in prion research. Given is a general overview about the technique itself and the broad spectrum of utilization as detection method for prions. The spontaneous generation of prions by the protein misfolding amplification (PMCA) are also discussed.

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  1. Institute for Neurodegenerative Diseases, University of California, 94143-0518, San Francisco, CA, USA

    Jan Stöhr

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  1. Inst. of Zoology, University of Mainz, Becherweg 6, Mainz, 55099, Germany

    J. Robin Harris

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Stöhr, J. (2012). Prion Protein Aggregation and FibrillogenesisIn Vitro . In: Harris, J. (eds) Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease. Subcellular Biochemistry, vol 65. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-5416-4_5

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