Fibril Formation by Short Synthetic Peptides
Nature produces an array of self-assembled fibres from proteins and peptides with a wide range of functionalities. This has inspired scientists to design peptides that exploit specific protein folds to form simple yet multi-functional self-assembled fibre
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Fibril Formation by Short Synthetic Peptides Andrew Smith
Abstract Nature produces an array of self-assembled fibres from proteins and peptides with a wide range of functionalities. This has inspired scientists to design peptides that exploit specific protein folds to form simple yet multi-functional selfassembled fibres. Of the various protein folds the most commonly used has been the β-sheet fold as it is easily accessible and produces nanoscale fibres which have a wide range of stabilities. Research has also been driven by the relationship to the various amyloid diseases, which produce β-sheet rich fibres. Here we will discuss the use of natural protein sequences as the basis of peptides that self-assemble to β-sheet rich fibres followed by peptide sequences that have been designed de novo purely based on the rules for the formation of a β-sheet. How changes in the amino acid sequence of these various peptides affects the properties of the fibres and also the macroscopic materials formed by these peptides will be discussed in each case. We will then look into how these structures have been utilized for applications as scaffolds for cell culture and tissue regeneration, followed by their use in the nanotechnology field. Keywords Self-assembly · De novo peptide · Beta-sheet · Peptide design
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Overview
In this chapter we will discuss the design and application of peptides that selfassemble into β-sheet structures reminiscent of the amyloid structure. Firstly I will introduce the field of peptide self-assembly and the various areas of research before concentrating on those peptides based on the β-sheet fold. These β-sheet peptides can be broken down into two groups, those based on naturally occurring sequences and those that are designed purely on the rules for forming β-sheets. For the natural sequences there are only a few examples of amyloid based sequences due to the obvious potential ramifications of using a sequence that can cause disease for applications. However, non-disease related sequences have been used to create beta-sheet based fibers. These natural sequences have been studied extensively and we will A. Smith () Lehrstuhl Biomaterialien, Universität Bayreuth, Universitätsstr. 30, 95440 Bayreuth, Germany e-mail: [email protected]
J. R. Harris (ed.), Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease, Subcellular Biochemistry 65, DOI 10.1007/978-94-007-5416-4_2, © Springer Science+Business Media Dordrecht 2012
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discuss the sequence-property relationship of those peptides specifically, the sequence-property relationships related to disease will be discussed elsewhere. The designed peptides purely utilize the rules for the β-sheet fold and self-assembly to generate a sequence whose properties can be varied by specific alterations to the amino acid sequence. Lastly we will discuss the varied applications of selfassembling β-sheet peptides in the fields of 3D cell culture, tissue regeneration and engineering and also nanotechnology.
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