Aggregation and Fibrillogenesis of Proteins not Associated with Disease: A Few Case Studies
While amyloid structures have been well characterised in a medical context, there is increasing interest in studying amyloid-like aggregates in other areas, such as food science and nanomaterials. Several proteins relevant to food processing, including se
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Aggregation and Fibrillogenesis of Proteins not Associated with Disease: A Few Case Studies Moritz Lassé, Juliet A. Gerrard and F. Grant Pearce
Abstract While amyloid structures have been well characterised in a medical context, there is increasing interest in studying amyloid-like aggregates in other areas, such as food science and nanomaterials. Several proteins relevant to food processing, including serum albumen, lactoglobulin, lysozyme, ovalbumin, casein, and soy protein isolate have been shown to form fibrillar structures under both physiological and non-physiological conditions. These structures are likely to contribute to the structural characteristics of the final food product. In a biotechnological context, proteins such as insulin and eye lens crystallins can be induced to form amyloid structures which can subsequently be used in biotechnology. One example of this is the use of amyloid fibrils as a scaffold for the immobilisation of enzymes. Another current interest in amyloid fibrils is as a storage form for peptide hormones, including insulin, glucagon and calcitonin. Here, we give an overview of a selection of well characterised proteins that have been studied outside the context of disease. Keywords Amyloid · Non-disease amyloid · Protein fibrils · Peptide fibrils · Fibrils · Food
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Introduction
In recent years, the formation of amyloid structures both in vivo and in vitro has become a major focus for research, especially in medical fields. This is because amyloid deposits play a significant role in many diseases. However, there is now a new trend of studying amyloid-like aggregates in other arenas, for example in food science and in nanomaterials science (Rajagopal and Schneider 2004; Greger 2008; F. G. Pearce () · M. Lassé · J. A. Gerrard Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, Private Bag 4800, Christchurch 8020, New Zealand e-mail: [email protected] M. Lassé e-mail: [email protected] J. A. Gerrard e-mail: [email protected] J. R. Harris (ed.), Protein Aggregation and Fibrillogenesis in Cerebral 253 and Systemic Amyloid Disease, Subcellular Biochemistry 65, DOI 10.1007/978-94-007-5416-4_11, © Springer Science+Business Media Dordrecht 2012
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MacPhee and Dobson 2000; Waterhouse and Gerrard 2004; Kroes-Nijboer et al. 2012; Gazit 2007). This is because amyloid aggregates display valuable characteristics including rheological behaviour, robustness, customisable surface chemistry, etc. The aim of this chapter is to briefly describe the mechanisms behind protein aggregation and to take a look at fibrillar protein aggregates that are not associated with disease. Aggregation usually is defined as the misfolding or unfolding of any protein or polypeptide with subsequent intermolecular interactions of the unfolded peptide regions. Since events in both the folding and unfolding process can lead to aggregation and potentially to fibrillogenesis, it is necessary to understand some of the ba
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