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SH3 Domains as Suitable Models to Study Amyloid Aggregation

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SH Domains

Abstract

Protein aggregation and amyloid fibril formation are related to a variety of neurodegenerative diseases for which no effective therapies or prevention methods exists yet. The study of well-characterized model proteins, even unrelated to disease, is a potent approach to investigate amyloid fibrils and in fact many of the advances in this intricate problem have been achieved from the study of model systems. In this chapter, we review the use of SH3 domains in the study of amyloid aggregation. We especially focus on the interest of combining biophysical techniques to quantitatively describe the kinetics of the different steps leading to fibrillation. Indeed, SH3 domains have been studied not only to elucidate the structural determinants of amyloid fibrils but also to unveil the thermodynamic and kinetic determinants of their formation precursors. Such contributions have given insight into the forces driving amyloid aggregation and may be of useful interest in future development of novel therapeutic or preventive strategies for neurodegenerative diseases.

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Abbreviations

Spc-SH3:

Src-homology region 3 domain of chicken α-spectrin

PI3-SH3:

SH3 domain of α-subunit of bovine phosphatidylinositol -3-kinase

NMR:

Nuclear magnetic resonance

TEM:

Transmission electron microscopy

AFM:

Atomic force microscopy

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Authors and Affiliations

  1. Facultad de Ciencias, Departamento de Química Física E Instituto de Biotecnología, Universidad de Granada, 18071, Granada, Spain

    Bertrand Morel, David Ruzafa & Francisco Conejero-Lara

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  1. Bertrand Morel
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  2. David Ruzafa
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  3. Francisco Conejero-Lara
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Correspondence to Bertrand Morel .

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  1. School of Theoretical Modeling, Washington, District of Columbia, USA

    Natalya Kurochkina

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Morel, B., Ruzafa, D., Conejero-Lara, F. (2015). SH3 Domains as Suitable Models to Study Amyloid Aggregation. In: Kurochkina, N. (eds) SH Domains. Springer, Cham. https://doi.org/10.1007/978-3-319-20098-9_1

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