2015
DOI: 10.2115/fiber.71.237
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Disulfide Cross-Linked Network Structure of Intermediate Filament and Matrix in Hair and Wool Cortices

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Cited by 4 publications
(3 citation statements)
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“…When wool fibers were dissolved and regenerated to form keratin film (KF), the diffraction peaks corresponding to crystal structure (α-helix structure and β -sheet structure) were remarkably reduced, and the proportion of amorphous region was increased. It was obviously indicated that the secondary structure of part of the keratin molecular chain was destroyed during the fiber dissolution process [35]. These molecular chains were disorderedly entangled together and eventually formed the amorphous region in the KF sample.…”
Section: Resultsmentioning
confidence: 99%
“…When wool fibers were dissolved and regenerated to form keratin film (KF), the diffraction peaks corresponding to crystal structure (α-helix structure and β -sheet structure) were remarkably reduced, and the proportion of amorphous region was increased. It was obviously indicated that the secondary structure of part of the keratin molecular chain was destroyed during the fiber dissolution process [35]. These molecular chains were disorderedly entangled together and eventually formed the amorphous region in the KF sample.…”
Section: Resultsmentioning
confidence: 99%
“…The disulfide bonds in cystine form a three-dimensionally linked network together with salt type bonds and hydrogen bonding. 9,10 It is well known that disulfide bonds have great bonding energy, making keratin's secondary structure difficult to damage easily, 11 so the wool fiber has higher stability and lower solubility. How to effectively break the disulfide bonds in the dissolving process while at the same time ensuring the protein macromolecule structure is not damaged or degraded too much is the key to obtaining high molecular weight keratin solution.…”
mentioning
confidence: 99%
“…The perm treatment process consists of two steps, the breaking of disulfide bonds in cysteine of protein by reducing agents and the restructuring of the disulfide bonds by oxidation. [9][10][11] Inspired by perm, it is a green and cleaner method to construct crosslinking structure based on disulfide bonds instead of adding the crosslinking agent. Disulfide bond is a chemical bond that drives from the sulfhydryl groups of two different cysteine residues in different peptide chains or the same peptide chain.…”
Section: Doi: 101002/mame202100498mentioning
confidence: 99%