Self-assembly of small peptide amphiphiles, the structures formed and their applications. (A foods and home and personal care perspective)

• Published in: Philosophical transactions of the Royal Society of London. Series A: Mathematical, physical, and engineering sciences physical, and engineering sciences, 2016-07, Vol.374 (2072), p.20150138
• Main Author: Frith, W. J.
• Format: Article
• Language: English
• Subjects: Amino Acids - chemistry; Fluorenes - chemistry; Food Industry; Gelation; Household Products; Hydrogels - chemical synthesis; Hydrogels - chemistry; Microfluidics; Peptide; Peptides - chemistry; Self-Assembly; Tyrosine - chemistry
• ISSN: 1364-503X; 1471-2962
• DOI: 10.1098/rsta.2015.0138

In this opinion piece, some specific challenges in the field of peptide self-assembly and gel formation are discussed. One major hurdle to finding functional small peptides is that there are a huge number of compounds to explore, which increases exponentially with the peptide size. This in itself creates a barrier to the discovery and application of materials, both through the difficulty of finding the peptides, and because protecting inventions also becomes more difficult. Recent work has shown that computer simulations may provide us a route to explore such a huge compound space; this is discussed along with the prospect for future developments. At the microscopic scale, many fibril-forming peptides form gels, apparently through a process of lateral association of primary self-assembled filaments, which leads to a relatively coarse-grained structure of rigid interconnects. However, recent data obtained on Fmoc-tyrosine gels appear to indicate that the gel microstructure is both more flexible and finer grained than previously believed. As such, it is clear that there is a considerable amount that is still not understood regarding this class of gel. This article is part of the themed issue ‘Soft interfacial materials: from fundamentals to formulation’.