2009
DOI: 10.1016/j.jcis.2009.04.050
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Wool keratin: A novel building block for layer-by-layer self-assembly

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Cited by 32 publications
(20 citation statements)
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“…Reduction and oxidation of disulfide bonds belong to the common methods for keratin isolation. Reduction of keratin involves use of 2‐mercaptoethanol (Balaji et al, ; Fujii & Li, ; Kakkar, Madhan, & Shanmugam, ; Reichl, ; Schrooyen, Dijkstra, Oberthür, Bantjes, & Feijen, ; Tanabe, Okitsu, & Yamauchi, ; Yamauchi, Yamauchi, Kusunoki, Kohda, & Konishi, ), dithiothreitol (DTT), dithioerythritol (Vasconcelos et al, ; Yang, Zhang, Yuan, & Cui, ), thioglycolic acid (Hill et al, ; Zabashta, Kasprova, Senchurov, & Grabovskii, ), glutathione (Schrooyen, Dijkstra, Oberthür, Bantjes, & Feijen, ), salts of hydrocyanic acid (Arai, Sakamoto, Naito, & Takahashi, ), bisulfites (Tonin et al, ), and m‐ bisulphites (Aluigi et al, ; Vasconcelos et al, ) to solubilize the protein. Many keratins can remain trapped within the protective structure, and usually a hydrogen‐bond breaking agent, such as urea, thiourea, transition metal hydroxides, surfactants, and combinations thereof, are included in the extractant to unfold or denature the protein (Torchinsky, ).…”
Section: Solubilization Of Keratinsmentioning
confidence: 99%
“…Reduction and oxidation of disulfide bonds belong to the common methods for keratin isolation. Reduction of keratin involves use of 2‐mercaptoethanol (Balaji et al, ; Fujii & Li, ; Kakkar, Madhan, & Shanmugam, ; Reichl, ; Schrooyen, Dijkstra, Oberthür, Bantjes, & Feijen, ; Tanabe, Okitsu, & Yamauchi, ; Yamauchi, Yamauchi, Kusunoki, Kohda, & Konishi, ), dithiothreitol (DTT), dithioerythritol (Vasconcelos et al, ; Yang, Zhang, Yuan, & Cui, ), thioglycolic acid (Hill et al, ; Zabashta, Kasprova, Senchurov, & Grabovskii, ), glutathione (Schrooyen, Dijkstra, Oberthür, Bantjes, & Feijen, ), salts of hydrocyanic acid (Arai, Sakamoto, Naito, & Takahashi, ), bisulfites (Tonin et al, ), and m‐ bisulphites (Aluigi et al, ; Vasconcelos et al, ) to solubilize the protein. Many keratins can remain trapped within the protective structure, and usually a hydrogen‐bond breaking agent, such as urea, thiourea, transition metal hydroxides, surfactants, and combinations thereof, are included in the extractant to unfold or denature the protein (Torchinsky, ).…”
Section: Solubilization Of Keratinsmentioning
confidence: 99%
“…Like many natural-derived biomaterials, keratin-based ones present poor mechanical strength. As a consequence, several approaches for controlling the physical and biological properties have been studied such as, blend systems with natural [58][59][60][61][62] and synthetic [33,63] polymers, use of crosslinking agents [64] and new preparation techniques [31,65,66]. Addition of chitosan to keratin forms strong and flexible films with improved swelling properties.…”
Section: Keratin Films and Coatingsmentioning
confidence: 99%
“…The biocompatibility was also demonstrated by cell adhesion and proliferation onto the films [31]. Recently, Yang et al described the use of keratin for layer-by-layer (LbL) self-assembly [66]. Herein, the film is formed by depositing alternating layers of oppositely charged materials.…”
Section: Keratin Films and Coatingsmentioning
confidence: 99%
“…Keratin hydrolyzates also find use in medicine, mainly for their similarity to human tissue. They are applied most when preparing films for tissue engineering when healing surface wounds (for example, chafes, burns) and as a substance supporting growth of new skin tissue 16,17 . Another medical application consists in making a composite material from polylactic acid and keratin and its utilization as frame for cultivating osteoblastsbone cells 18 .…”
mentioning
confidence: 99%