Self-assembling peptide literature

With a decade of experience, I have brought together seven papers with a scope limited to self-assembly of peptides, but covering key issues for advancing materials research into product development. The patent literature activity is typically an indicator of commercial interest and application space. Chapter 1 covers in some detail, but without being comprehensive, what self-assembled peptides may bring in terms of material applications. Chapters 2 and 3 explain the underlying principles of peptide self-assembly and how experiment can be used to model the hierarchy of structure formation. Typically, the work on peptides requires a tailored molecular... 

The following papers focus mainly on various aspects associated with the self-assembly of peptides. Peptides are relatively short sequences of amino acids, typically less than 50. The limited number of residues brings simplicity but still allows for sufficient differentiation to study self-assembly in its various details. The compositional freedom of the primary molecule allows for a sufficiently rich hierarchical structure creation through aggregation of individual peptides into supramolecular constructs resulting in interesting materials. This chapter looks into relevant patent literature as a reflection of the state of the art of technology in peptide self-assembly. 

Quickly browsing Internet resources with the keyword self-organization (or self-assembly, including the s and z versions) provides at least five hundred thousand links of varied relevance and quality. Searching the scientific literature for the same topics still provides about a hundred thousands "hits." Specifying further to peptides and proteins reduces the number of... 

As much of the more relevant scientific literature will be referenced in the subsequent papers, it is worthwhile examining the associated patent literature on peptide self-assembly. Patents are pursued to protect intellectual capital with the aim of developing science and technology into a business proposition. In the last 5 years, about 100 patents have been granted in the peptide self-assembly field with focus on applications in the medical and pharmaceutical markets. 

This review covers the literature on the aggregation of (homo)polypeptide hybrid copolymers and copolypeptides in dilute solution, which was published up to June 2005 a recent review on amphiphiles consisting of peptide sequences is given elsewhere in [12]. It was a particular concern to give a comprehensive overview on secondary structure effects in the self-assembly of these copolymers. Briefly presented are also structures in concentrated solutions (lyotropic phases) and in heterophase systems (see also [14]). 

In solution, peptide molecules adopt a specific secondary conformation, like P-sheet, P-hairpin, a-helix, or the coiled coil (Fig. 5.26). The secondary structures then self-assemble to form nanofibers or physically cross-linked networks. Elongation of the nanofibers in 3D space leads to thicker and longer fibers, which further assemble to fibrillar networks capable of entrapping water (Fig. 5.25) [55]. P-Structured peptides dominate the literature of self-assembled systems, either natural or designed. 

Supramolecular materials are architectures consisting of molecules that are able to self-assemble into larger constructs (Lehn, 2002). Polymers as well as small molecules are able to form self-assembled structures. Supramolecular materials based on small molecules such as peptides or peptide amphiphiles are also referred to as supramolecular polymers. Despite the importance of enzyme controlled self-assembly of small molecules, these materials will not be discussed here as they are not based on conventional polymers. More information on these materials can be found in the recent literature (Roy and Ulijn, 2010 Zelzer et al., 2013). 

Another interesting application was given for diselenide-based block copolymers, where both oxidants as well as reductants forced the systems to a demicellization [275]. This system was further developed to allow the disassembly of the micelles by apphcation of oxidants, whereas micellization was favored in the presence of reductants [276]. In continuation, selenium-based peptides and dendrimers self-assembled into different morphologies, depending on the oxidation state [277, 278]. Also, small selenium-based amphiphiles form complexes with polyelectrolytes, but the amphiphihc character of the amphiphile and - in turn - the complex decreases after oxidation [279]. In general, the literature contains a... 

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