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Fig. 1 Proposed oxidation breakdown pathway for wool keratin drawn in ChemDraw (version 15.1) [9, 10].
A key feature of the chemical structure of wool keratin proteins is their high cystine content.
Regenerated wool keratin is a promising natural material for tissue engineering.
The intramolecular and intermolecular disulfide network is a significant component of the wool keratin cellular substructure [8].
As a natural protein, wool keratin was used to improve the cell affinity of poly l-lactic acid) (poly l-lactic
The forming and coverage of nanonets was mainly affected by the addition of wool keratin and the relative humidity.
Similar(49)
The mechanism for the process of disulfide oxidation in wool keratins is uncertain.
NIR spectra were analysed over the spectral range of 1400 2400 nm to remove the effects of dyed samples and to exclude regions where peaks related to wool keratins were not found [46, 47].
Historically, keratin research started with studies of sheep hair (wool) keratins (Crick 1952; Powell and Rogers 1986; Oshima 2007).
The subcomponents were then utilised to form wool-keratin structures, using a keratin extract as the matrix.
Mats of wool-derived keratin nanofibre have been prepared by electrospinning solutions of keratin in formic acid at 20 and 15 wt.%, and obtaining nanofibres with mean diameter of about 400 and 250 nm, respectively.
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