Crosslinking structure of keratin: III. Rubberlike elasticity originating from non‐uniform structures of the swollen hair and wool fibers

Arai, Kozo; Ma, Guanghui; Hirata, Taishi

doi:10.1002/app.1991.070420426

Cited by 11 publications

(11 citation statements)

References 17 publications

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“…Mechanical tests for swollen fibers were performed according to previously described methods [8,9]. A swollen fiber sample of about 20 mm in length was set between the sample holders in a liquid cell.…”

Section: Force-extension Curve For Swollen Keratin Fibersmentioning

confidence: 99%

“…proteins by hydrogen bond scission [11]. When such a non-uniform structure is stretched, microdomains of KAP serve as reinforcing filler particles in rubber [8].…”

Section: Reversibility In the Stress-strain Curves For Swollen And Dementioning

confidence: 99%

“…NonGaussian chain statistics were applied to the stretched swollen sample, and a theoretical relation between the equilibrium force F and the extension ratio α of the rubber phase was derived as follows : [8,23] …”

Section: A Mechanical Model For the Extension Of Swollen Fibermentioning

confidence: 99%

“…In the case of hair and wool keratin, a near spherical particle is assumed ; i.e., 1!κ!2. According to Guth [24] and Leonard [25], the filler effect can be expressed by equation (4) [8] as follows :…”

Section: A Mechanical Model For the Extension Of Swollen Fibermentioning

confidence: 99%

“…A mechanical method for analyzing the number, type, and location of SS cross-links in the keratin cortex has been developed by the authors [8][9][10][11]. This method is based on the application of a nonGaussian elastic equation of state to the stress-strain curve of a swollen fiber.…”

Section: Introductionmentioning

confidence: 99%

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Disulfide Cross-Linked Network Structure of Intermediate Filament and Matrix in Hair and Wool Cortices

Suzuta

Arai²

2015

Sen-i Gakkaishi

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Section: Force-extension Curve For Swollen Keratin Fibersmentioning

confidence: 99%

“…proteins by hydrogen bond scission [11]. When such a non-uniform structure is stretched, microdomains of KAP serve as reinforcing filler particles in rubber [8].…”

Section: Reversibility In the Stress-strain Curves For Swollen And Dementioning

confidence: 99%

Section: A Mechanical Model For the Extension Of Swollen Fibermentioning

confidence: 99%

Section: A Mechanical Model For the Extension Of Swollen Fibermentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Disulfide Cross-Linked Network Structure of Intermediate Filament and Matrix in Hair and Wool Cortices

Suzuta

Arai²

2015

Sen-i Gakkaishi

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Characterization of cross-links introduced in gelatin

Honda

Arai

Mitomo

1997

J. Appl. Polym. Sci.

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A method for the determination of the effectiveness of gelatin hardeners was proposed. Formaldehyde (FA) and 1,3-bis(vinylsulfonyl)-2-propanol (BVSP) were used as cross-linking agents for the hardening of gelatin. The cross-linked gelatin showed a typical rubber elasticity in a swollen state with a mixed solution composed of concentrated aqueous LiBr and diethylene glycol monoalkyl ether. The energy components to total retractive forces were below 0.3. The amount of intermolecular crosslinks was estimated by applying an usual rubber elasticity theory for the swollen samples. The number of cross-linking sites was also determined by the amino acid analysis of BVSP cross-linked gelatin. The cross-linking efficiency for the reaction of BVSP occurring in a casting film with less swelling conditions was about four times higher than in a swollen gel. Approximately 92% or more of BVSP used was reacted with the free amino groups of lysine and arginine residues. There was a significant difference between the reactivities of these amino groups. The amino groups of lysine residues were more reactive than those of arginine in a gel state; the reactivities, however, reversed in a thin layer of wet film. The effectiveness of FA was extremely low.

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Cross‐linking structure of keratin. IV. The number of cross‐linkages in low‐sulfur components and the volume fraction of high‐sulfur domains in various α‐keratin fibers

Arai

Hirata

Nishimura

et al. 1993

J of Applied Polymer Sci

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SYNOPSISVarious a-keratin fibers that had been treated with an 11 M LiBr solution containing Nethylmaleimide showed typical rubberlike elasticity in a solution composed of equal volumes of 8M LiBr and diethylene glycol mono-n-butyl ether. Stress-strain relations of the swollen fibers were treated with a two-phase model: a mechanically stable phase of higher crosslinked domains and a rubber phase with lower cross-link density. Stress-strain curves for a variety of keratins (three different human hairs, six different wools, mohair, cashmere, llama, alpaca, angora, and opossum) were analyzed by applying non-Gaussian chain statistics to the swollen keratin network, including microdomains, which act as reinforcing filler particles in rubber. The phase structures of unswollen domains and swollen rubber were considered to originate from different structural components characteristic of a-keratin, namely, the high-sulfur matrix and the low-sulfur microfibrils being randomized by swelling. It has been suggested that ( 1 ) the modulus of swollen fibers increases with increase of the content of disulfide (SS) in keratins, ( 2 ) the volume fraction of high-sulfur domains increases with increase of SS content, and ( 3 ) the number of intermolecular cross-links in the rubber region of low-sulfur proteins is virtually the same among keratins and reaches about 65-75% of the SS linkages in the corresponding proteins. Some discussion has been made on the SS bonding in situ, namely, SS linkages between the low-sulfur proteins, between the low-sulfur and the high-sulfur proteins, and between the high-sulfur proteins in keratins. 0

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Crosslinking structure of keratin: III. Rubberlike elasticity originating from non‐uniform structures of the swollen hair and wool fibers

Cited by 11 publications

References 17 publications

Disulfide Cross-Linked Network Structure of Intermediate Filament and Matrix in Hair and Wool Cortices

Disulfide Cross-Linked Network Structure of Intermediate Filament and Matrix in Hair and Wool Cortices

Characterization of cross-links introduced in gelatin

Cross‐linking structure of keratin. IV. The number of cross‐linkages in low‐sulfur components and the volume fraction of high‐sulfur domains in various α‐keratin fibers

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