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Hair is a proteinaceous fibre with a strongly hierarchical organization of subunits, from the alpha-keratin chains, via intermediate filaments, to the fibre. The chemistry of the different morphological compartments results in exciting physical properties, including the hydrophilic/hydrophobic paradox. The present tutorial review will be of interest for protein- as well as polymer chemists, who want to learn from nature, and also for biochemists interested in the cytoskeleton and particularly in intermediate filaments; it also presents a scientific basis for hair cosmetics.

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The thermal transition of a thermoresponsive microgel of poly‐N‐isopropylacrylamide (PNIPAM; transition temperature=34 °C) is shifted to higher temperatures when it is embedded in a shell of temperature‐sensitive poly‐N‐isopropylmethacrylamide (PNIPMAM; transition temperature=44 °C). The magnitude of the shift depends on the shell/core mass ratio. A thick shell induces a third transition arising from strong mechanical forces exerted on the core.

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Keratins are self-organized proteins that are abundantly available in wool, feather, human hair, etc., making them a potential cheap feedstock for the modification of amino acids. This paper explores the hydrolysis of keratin in water under specific pressure-temperature conditions where the hydrolysis through scission of the protein chain yields oligopeptides. Here we report for the first time that, under appropriate conditions, these oligopeptides self-assemble into a hierarchical architecture, the process being followed in time by optical microscopy. Birefringent needle-like crystals are observed which tend to nucleate heterogeneously. When given sufficient time, these needles become tens of microns in length and act as further nuclei, developing a highly repetitive structure of several hundreds of microns in size. Micro-focus X-ray diffraction studies supported by in situ microscopy reveal that these needles have a crystal structure similar to that of the native protein, although better organized along the ab-plane. Spectroscopic studies on these structures show crystalline bands that disappear above 150 degrees C, coinciding with an endothermic peak in DSC. Amino acid analysis shows that the self-assembled birefringent entities are indeed oligopeptides, consisting of sequences of approximately 40 amino acids. The proposed ecofriendly route provides an effective route for obtaining oligopeptides that can be used as important building blocks for the synthesis of a range of novel polymers. The oligopeptides obtained from the sustainable source can be used as important building blocks for the synthesis of a range of novel polymers.

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