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Protein Design pp 277–293Cite as

Protein Misfolding Disorders and Rational Design of Antimisfolding Agents

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Part of the book series: Methods in Molecular Biology ((MIMB,volume 340))

Abstract

Compelling evidence strongly suggests that the conversion of a normal soluble protein into a β;-sheet–rich oligomeric structure and further fibril formation is the critical step in the pathogenesis of several human diseases, termed protein misfolding disorders. Therefore, a promising therapeutic strategy consists of the design of molecules that prevent the misfolding and aggregation of these proteins. In this chapter, we survey the mechanism of protein misfolding and some strategies to rationally produce inhibitors of this process.

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Author information

Authors and Affiliations

  1. Protein Misfolding Disorders Laboratory, Department of Neurology, University of Texas Medical Branch, Galveston, TX

    Lisbell D. Estrada, June Yowtak & Claudio Soto

Authors
  1. Lisbell D. Estrada
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  2. June Yowtak
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  3. Claudio Soto
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Editor information

Editors and Affiliations

  1. Département de Biologie Joliot–Curie CEA Saclay, Gif-sur-Yvette, France

    Raphael Guerois

  2. Merz Pharmaceuticals GmbH, Frankfurt am Main, Germany

    Manuela López de la Paz

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© 2006 Humana Press Inc.

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Estrada, L.D., Yowtak, J., Soto, C. (2006). Protein Misfolding Disorders and Rational Design of Antimisfolding Agents. In: Guerois, R., de la Paz, M.L. (eds) Protein Design. Methods in Molecular Biology, vol 340. Humana Press. https://doi.org/10.1385/1-59745-116-9:277

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  • DOI: https://doi.org/10.1385/1-59745-116-9:277

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-585-9

  • Online ISBN: 978-1-59745-116-1

  • eBook Packages: Springer Protocols

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